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BBA - Proteins and Proteomics (v.1794, #6)

Editorial Board (pp. i).

Structural and thermodynamic analysis of thrombin:suramin interaction in solution and crystal phases by Luis Maurício T.R. Lima ⁎; Camila Franco Becker; Guilherme Menegon Giesel; Adriana Fonseca Marques; Maria Thereza Cargnelutti; Mario de Oliveira Neto; Robson Queiroz Monteiro; Hugo Verli; Igor Polikarpov ⁎ (pp. 873-881).

Suramin is a hexasulfonated naphthylurea which has been recently characterized as a non-competitive inhibitor of human alpha-thrombin activity over fibrinogen, although its binding site and mode of interaction with the enzyme remain elusive. Here, we determined two X-ray structure of the thrombin:suramin complex, refined at 2.4 Å resolution. While a single thrombin:suramin complex was found in the asymmetric unit cell of the crystal, some of the crystallographic contacts with symmetrically related molecules are mediated by both the enzyme and the ligand. Molecular dynamics simulations with the 1:1 complex demonstrate a large rearrangement of suramin in the complex, but with the protein scaffold and the more extensive protein–ligand regions keep unchanged. Small-angle X-ray scattering measurements at high micromolar concentration demonstrate a suramin-induced dimerization of the enzyme. These data indicating a dissimilar binding mode in the monomeric and oligomeric states, with a monomeric, 1:1 complex to be more likely to exist at the thrombin physiological, nanomolar concentration range. Collectively, close understanding on the structural basis for interaction is given which might establish a basis for design of suramin analogues targeting thrombin.

Keywords: Abbreviations; TBS; tris-buffered saline (20 mM Tris–HCl, 150 mM NaCl, pH 7.5); FPRCK; D-Phe-Pro-Arg-cloromethylketone-α-thrombin; Suramin; 8, 8′-[carbonylbis[imino-3,1-phenylenecarbonylimino(4-methyl-3,1-phenylene)carbonylimino]]bis-1,3,5-naphthalenetrisulfonic acidThrombin; Suramin; Crystallography; Molecular dynamic simulation; Small-angle X-ray scattering

Urine proteomic profiling of uranium nephrotoxicity by Véronique Malard ⁎; Jean-Charles Gaillard; Frédéric Bérenguer; Nicole Sage; Eric Quéméneur (pp. 882-891).

Uranium is used in many chemical forms in civilian and military industries and is a known nephrotoxicant. A key issue in monitoring occupational exposure is to be able to evaluate the potential damage to the body, particularly the kidney. In this study we used innovative proteomic techniques to analyse urinary protein modulation associated with acute uranium exposure in rats. Given that the rat urinary proteome has rarely been studied, we first identified 102 different proteins in normal urine, expanding the current proteome data set for this central animal in toxicology. Rats were exposed intravenously to uranyl nitrate at 2.5 and 5 mg/kg and samples were collected 24 h later. Using two complementary proteomic methods, a classic 2-DE approach and semi-quantitative SDS-PAGE-LC-MS/MS, 14 modulated proteins (7 with increased levels and 7 with decreased levels) were identified in urine after uranium exposure. Modulation of three of them was confirmed by western blot. Some of the modulated proteins corresponded to proteins already described in case of nephrotoxicity, and indicated a loss of glomerular permeability (albumin, alpha-1-antiproteinase, serotransferrin). Others revealed tubular damage, such as EGF and vitamin D-binding protein. A third category included proteins never described in urine as being associated with metal stress, such as ceruloplasmin. Urinary proteomics is thus a valuable tool to profile uranium toxicity non-invasively and could be very useful in follow-up in case of accidental exposure to uranium.

Keywords: Abbreviations; CEA; Commissariat à l'Energie Atomique; DSV; Direction des Sciences du Vivant; IBEB; Institut de Biologie Environnementale et de Biotechnologie; SBTN; Service de Biochimie et Toxicologie Nucléaire; BUN; blood urea nitrogenMass spectrometry; Toxicology; Toxicoproteomics; Uranium; Urine

Characterization of the S289A,D mutants of yeast cystathionine β-synthase by Faraz Quazi; Susan M. Aitken ⁎ (pp. 892-897).

Cystathionine β-synthase (CBS) catalyzes the pyridoxal 5′-phosphate (PLP)-dependent condensation ofl-serine andl-homocysteine to forml-cystathionine in the first step of the reverse transsulfuration pathway. Residue S289 of yeast CBS, predicted to form a hydrogen bond with the pyridine nitrogen of the PLP cofactor, was mutated to alanine and aspartate. Thek_cat/K_ml ^-Ser of the S289A mutant is reduced by a factor of ∼800 and the β-replacement activity of the S289D mutant is undetectable. Fluorescence energy transfer between tryptophan residue(s) of the enzyme and the PLP cofactor, observed in the wild-type enzyme and diminished in the S289A mutant, is absent in S289D. These results demonstrate that residue S289 is essential in maintaining the properties and orientation of the pyridine ring of the PLP cofactor. The reduction in activity of ytCBS-S289A suggests that ytCBS catalyzes the α,β-elimination ofl-Ser via an E1cB mechanism.

Keywords: Abbreviations; AA; aminoacrylate; l; -Cth; l; -cystathionine; CBL; cystathionine β-lyase; CBS; cystathionine β-synthase; hCBS; human CBS; yCBS; yeast CBS; ytCBS; truncated yCBS (residues 1–353); DTNB; 5,5′-dithio-bis-(2-nitrobenzoic acid); l; -Hcys; l; -homocysteine; LDH; l; -lactate dehydrogenase; OAS; O; -acetyl-; l; -serine; OASS; O; -acetylserine sulfhydrylase; PLP; pyridoxal 5′-phosphate; TrpS; tryptophan synthaseCystathionine; Pyridoxal 5′-phosphate; Mechanism

Altered secretome of Burkholderia pseudomallei induced by salt stress by Pornpan Pumirat; Putita Saetun; Supachok Sinchaikul; Shui-Tein Chen; Sunee Korbsrisate ⁎; Visith Thongboonkerd ⁎ (pp. 898-904).

Burkholderia pseudomallei is a saprophyte found in soil and water. It is a difficult microorganism to kill and can survive in these environments for many years. Mechanisms for its adaptive response to environmental changes remain largely unknown. We performed a proteomics study to examine alterations in secreted proteins (secretome) under a salt stress (with 150 mM NaCl) compared to the normal cultured condition in LB broth. The culture supernatants were filtrated and precipitated with 50% ethanol. The isolated proteins were recovered, separated with 2-D PAGE, and visualized with SYPRO Ruby stain ( n=5 gels for each group). Differentially expressed protein spots were identified by Q-TOF MS and/or MS/MS analyses. A total of 42 protein spots representing 37 unique proteins were identified as the altered proteins during the salt stress, including metabolic enzymes, transcription/translation regulators, potential virulence factors, chaperones, phage capsid proteins, drug resistance protein, solute transport regulator, and hypothetical proteins. The presence of secreted GroEL only after NaCl exposure was confirmed by Western blot analysis. The increased level (19-fold) of a beta-lactamase-like protein suggested that the NaCl-exposed bacterium might resist to beta-lactam antibiotics. Functional analysis revealed that the NaCl-exposed bacterium had significantly greater survival rate after a treatment with ceftazidime. Our study provided the first dataset of the secretome of B. pseudomallei and its alterations, which may lead to novel insights into adaptive response of B. pseudomallei during the salt stress.

Keywords: Adaptive response; Burkholderia pseudomallei; Melioidosis; Proteome; Proteomics; Salt stress; Secretome

Attenuation of ionic interactions profoundly lowers the kinetic thermal stability of Pyrococcus furiosus triosephosphate isomerase by Sanjeev Kumar Chandrayan; Purnananda Guptasarma ⁎ / (pp. 905-912).

We investigate here the high structural stability of Pyrococcus furiosus triosephosphate isomerase (PfuTIM) by exploring the effects – upon the protein's structure and kinetic thermal stability – of modulation of its ionic interactions through pH variations, and mutations. PfuTIM shows comparable structural contents at pH 3.0, 7.0 and 10.0. However, at pH 3.0, subtle changes are seen in the protein's surface hydrophobicity and association status, and its kinetic thermal stability is profoundly reduced (as evidenced by its facile heat- and cold-mediated denaturation, characterized by a high degree of hysteresis and irreversibility). Increase in ionic strength through addition of salt counters the reduction of stability, and reversal of pH facilitates partial refolding. Further, a mutated form of PfuTIM (mPfuTIM) lacking 4 key charged residues involved in ionic interactions displays a structural content identical to PfuTIM but profound reduction in kinetic stability to thermal and chemical denaturation, as well as evidence of partial unfolding at temperatures between 90 °C and 100 °C, unlike PfuTIM. We conclude, therefore, that ionic interactions (which are known to determine protein thermodynamic stability) can also contribute significantly to protein kinetic thermal stability.

Keywords: Protein thermal stability; Protein unfolding; Kinetic stability; Cold denaturation; Salt bridge and ionic interaction

Suppression of lysozyme aggregation at alkaline pH by tri- N-acetylchitotriose by Satish Kumar; Vijay Kumar Ravi; Rajaram Swaminathan ⁎ (pp. 913-920).

Inhibiting protein misfolding and aggregation is imperative for treatment of amyloid diseases. In this regard small molecules which bind to and stabilize the monomeric protein have invited attention owing to their ability to significantly slow down or inhibit aggregation and amyloid formation. We have earlier shown that hen egg-white lysozyme (HEWL) spontaneously forms soluble oligomers at pH 12.2, which are later stabilized by intermolecular disulphide bonds, eventually resulting in amyloid fibrils. In this work, we show that overnight (∼12 h) pre-incubation of HEWL with its competitive inhibitor, N, N′, N″-Triacetylchitotriose (chitotriose) at neutral pH, impairs its aggregation and fibrillogenesis at pH 12.2. Unlike in control or N-Acetyl-D-glucosamine (NAG) pre-incubated samples, HEWL–chitotriose complex displayed i) reduced thioflavin T and ANS fluorescence, ii) small oligomers but no amyloid fibrils in AFM, iii) absence of large aggregates in SDS-PAGE and gel-filtration elutions, iv) marginally more helical content in CD spectra and v) >70% enzymatic activity after 24 h and ∼16% activity after week long incubation at alkaline pH. It is likely that strong binding in the HEWL–chitotriose complex, in contrast to weakly bound HEWL–NAG complex, raises the activation energy barrier for protein misfolding and subsequent aggregation, thereby retarding the aggregation kinetics substantially. These results hold promise for the therapy of human lysozyme amyloidosis.

Keywords: Abbreviations; HEWL; hen egg white lysozyme; chitotriose; N; ,; N; ′,; N; ″-Triacetylchitotriose; ThT; Thioflavin T; ANS; 8-Anilino-1-naphthalene sulfonic acid; NAG; N; -Acetyl-; d; -glucosamine; SDS; sodium dodecyl sulfate; SDS-PAGE; SDS polyacrylamide gel electrophoresis; DTT; dithiothreitol; DTNP; 2,2′-dithiobis(5-nitropyridine); min; minutes; h; hoursInhibitor; Enzyme activity; Amyloid fibril; Atomic force microscopy; Thioflavin T; Protein stabilization; SDS PAGE

Differential stabilities of alternative exon-skipped rod motifs of dystrophin by Chris Ruszczak; Ahmed Mirza; Nick Menhart ⁎ (pp. 921-928).

Exon skipping repair is a strategy being investigated in early stage clinical trials to treat Duchenne muscular dystrophy. This is most applicable to the majority of cases which arise when genetic defects cause frame shift mutations, and induced exon skipping of out-of-phase exons restores the reading frame. However, the consequences to the edited protein so produced have not been considered. In many cases alternative routes to restoring the reading frame are possible, and we show in a test case involving exon 44 that the resulting differently edited proteins greatly vary in stability, with one of them very similar to normal unskipped dystrophin, and the other much less stable as assessed by the thermodynamics of folding as well as resistance to proteolysis. This has implications for the design of optimal therapeutic exon skipping strategies, which presumably wish to result repairs with as much fidelity to normal dystrophin as possible.

Keywords: Abbreviations; DMD; Duchenne muscular dystrophy; BMD; Becker muscular dystrophy; STR; spectrin type repeat; Dx; a protein composed of the xth STR motif of dystrophin; Dx:y; a protein spanning the xth to the yth STR of dystrophin; D16:18Δe43,44; or equivalently in figures for brevity; Δe43,44; : D16:18 with the region coding for exons 43 and 44 deleted; D16:18Δe44,45; or equivalently; Δe44,45; : D16:18 with the region coding for exons 44 and 45 deletedDystrophin; Exon skipping; Spectrin type repeat; Stability

Glycine betaine may have opposite effects on protein stability at high and low pH values by Laishram R. Singh; Tanveer Ali Dar; Safikur Rahman; Shazia Jamal; Faizan Ahmad ⁎ (pp. 929-935).

The compatible osmolyte glycine betaine (GB) is the most efficient osmoprotectant and best excluder from the protein surface. It can reverse protein aggregation and correct mutant protein defects and counter the harmful effects of urea and salts in vivo and in vitro. In this study we have investigated the pH dependence of the stabilizing effect of GB on three different proteins, namely, α-lactalbumin (α-LA), lysozyme and ribonuclease-A (RNase-A). We show here that (a) GB stabilizes RNase-A at all pH values, and (b) GB has opposite effects on two proteins at high pH and low pH values, namely, α-LA and lysozyme. This conclusion was reached by determining T_m (midpoint of denaturation), Δ H_m (denaturational enthalpy change at T_m), Δ C_p (constant-pressure heat capacity change) and Δ G_D^o (denaturational Gibbs energy change at 25 °C) of proteins in the presence of different GB concentrations. Another conclusion of this study is that Δ H_m and Δ C_p are not significantly changed in the presence of GB. This study suggests that other methylated glycine osmolytes may also behave in the same manner.

Keywords: Osmolyte; Protein stability; Glycine betaine; Protein denaturation; Preferential hydration; Free energy change

Polyglutamine tract binding protein-1 is an intrinsically unstructured protein by Masaki Takahashi; Mineyuki Mizuguchi ⁎; Hiroyuki Shinoda; Tomoyasu Aizawa; Makoto Demura; Hitoshi Okazawa; Keiichi Kawano (pp. 936-943).

Polyglutamine tract binding protein-1 (PQBP-1) is a nuclear protein that interacts with disease proteins containing expanded polyglutamine repeats. PQBP-1 also interacts with RNA polymerase II and a spliceosomal protein U5-15kD. In the present study, we demonstrate that PQBP-1 is composed of a large unstructured region and a small folded core. Intriguingly, the large unstructured region encompasses two functional domains: a polar amino acid rich domain and a C-terminal domain. These findings suggest that PQBP-1 belongs to the family of intrinsically unstructured/disordered proteins. Furthermore, the binding of the target molecule U5-15kD induces only minor conformational changes into PQBP-1. Our results suggest that PQBP-1 includes high content of unstructured regions in the C-terminal domain, in spite of the binding of U5-15kD.

Keywords: Abbreviations; ANS; 1-anilino-8-naphtalenesulfonate; CD; circular dichroism; CTD; C-terminal domain; DRPLA; dentatorubro-pallidoluysian atrophy; DTT; dithiothreitol; GdnHCl; guanidine hydrochloride; HSQC; heteronuclear single-quantum correlation; Pol II; RNA polymerase II large subunit; PONDR; predictors of natural disordered regions; POODLE-L; prediction of order and disorder by machine learning-L; PQBP-1; polyglutamine tract binding protein-1; PRD; polar amino acid rich domain; SCA; spinocerebellar ataxia; WWD; WW domainUnstructured protein; Protein structure; PQBP-1; Polyglutamine; U5-15kD

Structural rearrangements and the unfolding mechanism of a Trigger Factor mutant studied by multiple structural probes by Dong-Jie Fan; Yan-Wei Ding; Jun-Mei Zhou ⁎ (pp. 944-952).

Trigger Factor (TF) is a three-domain chaperone which catalyzes nascent peptide folding and harbors peptidyl–prolyl cis–trans isomerase activity. The multi-domain structure of TF makes it an interesting and challenging candidate for studies of the structural properties and functional behavior of individual domains or combined domain constructs. Here we constructed a TF mutant, NC, combining the N- and C-domains that are responsible for TF's chaperone function, and compared structural changes and unfolding characteristics of NC with wild-type TF by monitoring fluorescence spectra, far-UV CD, chemical crosslinking, DSC and binding with hydrophobic probes (ANS or bis-ANS). The results showed that the NC construct, like intact TF, could bind to hydrophobic probes, form dimers in solution, and showed a similar 3-state guanidine-induced unfolding profile. However, the NC fragment showed reduced stability towards both guanidine unfolding and thermal denaturation, suggesting that the presence of the M-domain of TF contributes to the stability of the intact TF structure.

Keywords: Abbreviations; TF; Trigger Factor; NC; a Trigger Factor fragment consisting of its N- and C-domains; bis-ANS; 4,4′-bis(1-anilino-8-naphthalenesulfonic acid); DSC; differential scanning calorimetry; DSS; disuccinimidyl suberate; GuHCl; guanidine hydrochloride; CD; circular dichroism; DTSP; dithiobis succinimidyl propionate; GAPDH; d; -glyceraldehyde-3-phosphate dehydrogenaseTrigger Factor; CD; ANS; bis-ANS; Differential scanning calorimetry; Intermediate; Protein folding

Crystal structures of T. vivax nucleoside hydrolase in complex with new potent and specific inhibitors by Wim Versées; Annelies Goeminne; Maya Berg; An Vandemeulebroucke; Achiel Haemers; Koen Augustyns; Jan Steyaert (pp. 953-960).

Diseases caused by parasitic protozoa remain a major health problem, mainly due to old toxic drugs and rising drug resistance. Nucleoside hydrolases are key enzymes of the purine salvage pathway of parasites from the Trypanosomatidae family and are considered as possible drug targets. N-Arylmethyl substituted iminoribitols have been developed as selective nanomolar affinity inhibitors against the purine-specific nucleoside hydrolase of Trypanosoma vivax. The current paper describes the crystal structures of the T. vivax nucleoside hydrolase in complex with two of these inhibitors, to 1.3 and 1.85 Å resolution. These high resolution structures provide an accurate picture of the mode of binding of these inhibitors and their mechanism of transition-state mimicry, and are valuable tools to guide further inhibitor design. Comparison of the current structures with previously solved structures of the enzyme in complex with ground-state and transition-state-analogue inhibitors also allows for the elucidation of a detailed molecular mechanism of active-site loop opening/closing. These loop movements can be coupled to the complex kinetic mechanism of the T. vivax nucleoside hydrolase.

Keywords: Abbreviations; IAG-NH; inosine–adenosine–guanosine preferring nucleoside hydrolase; IU-NH; inosine–uridine preferring nucleoside hydrolase; TvNH; nucleoside hydrolase from; Trypanosoma vivax; TvNH-InhB; TvNH in complex with compound; B; ((2; R; ,3; R; ,4; S; )-1-[(4-hydroxy-5; H; -pyrrolo[3,2-; d; ]pyrimidin-7-yl)methyl]-2-(hydroxymethyl)pyrrolidin-3,4-diol); TvNH-InhD; TvNH in complex with compound; D; ((2; R; ,3; R; ,4; S; )-2-(hydroxymethyl)-1-(quinolin-8-ylmethyl)pyrrolidin-3,4-diol); TvNH-ImmH; TvNH in complex with Immucillin H (compound; A; ); rmsd; root mean square deviation; ImmH; immucillin H or [(1; S; )-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-; d; -ribitol]; DADMe-ImmH; 4′-deaza-1′-aza-2′-deoxy-1′-(9-methylene)-immucillinHNucleoside hydrolase; Inhibitor design; Transition state inhibitor; Iminoribitol; Leaving group activation; Loop movement

Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics by Virendar K. Kaushik ⁎; Michael Kavana; Jessica M. Volz; Stephen C. Weldon; Susan Hanrahan; Jian Xu; Shari L. Caplan; Brian K. Hubbard (pp. 961-967).

Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA, a key metabolite in the fatty acid synthetic and oxidation pathways. The present study describes the steady-state kinetic analysis of a purified recombinant human form of the enzyme, namely ACC2, using a novel LC/MS/MS assay to directly measure malonyl-CoA formation. Four dimensional matrices, in which bicarbonate (HCO₃⁻), ATP, acetyl-CoA, and citrate were varied, and global data fitting to appropriate steady-state equations were used to generate kinetic constants. Product inhibition studies support the notion that the enzyme proceeds through a hybrid (two-site) random Ter Ter mechanism, one that likely involves a two-step reaction at the biotin carboxylase domain. Citrate, a known activator of animal forms of ACC, activates both by increasing k_cat and k_cat/ K_M for ATP and acetyl-CoA.

Keywords: Abbreviations; ACC; acetyl-CoA carboxylase; HPLC; high pressure liquid chromatography; LC/UV; liquid chromatography/ultraviolet detection; LC/MS/MS; liquid chromatography/mass spectrometry/mass spectrometry; ESI; electrospray ionization; MRM; multiple reaction monitoring; m; /; z; mass-to-charge; C12E8; octaethylene glycol monododecyl ether; HCO; ₃; ⁻; bicarbonate; ATP; adenosine 5′-triphosphate; Mg-ATP; Mg-ATP; ²⁻; complex; Mg-citrate; Mg-citrate; ⁻; complex; CoA; coenzyme A; P; _i; inorganic phAcetyl-CoA carboxylase; Malonyl-CoA; Steady-state kinetics

Deregulation of allosteric response of Lactococcus lactis prolidase and its effects on enzyme activity by Guodong Zhang; Jian An Chen; Takuji Tanaka (pp. 968-975).

The allosteric behaviour of Lactococcus lactis prolidase (Xaa-Pro dipeptidase) of this proline-specific peptidase was investigated where it was hypothesized that intersubunit interactions between a loop structure and three residues near the active site contributed to this behaviour. Seven mutant prolidases were constructed, and it was observed that the loopless mutant and His303 substitution inactivated the enzyme. Ser307 substitution revealed that this residue influenced the substrate binding, as judged from its kinetic constants and substrate specificity; however, this residue did not contribute to allostery of prolidase. R293S mutation resulted in the disappearance of the allosteric behaviour yielding a Hill constant of 0.98 while the wild type had a constant of 1.58. In addition, the R293S mutation suppressed the substrate inhibition that was observed in other mutants and wild type. The K_m value of R293S was 2.9-fold larger and V_max was approximately 50% less as compared to the wild type. The results indicated that Arg293 increased the affinity for substrates while introducing allosteric behaviour and substrate inhibition. Computer modelling suggested that negative charges on the loop structure interacted with Arg293 and Ser307 to maintain these characteristics. It was, therefore, concluded that Arg293, His303, Ser307 and the loop contributed to the enzyme's allosteric characteristics.

Keywords: Peptidase; Proline; Bitterness; Flexible loop; Proteolysis; Protein engineering

Cloning and characterization of Lotus japonicus formate dehydrogenase: A possible correlation with hypoxia by A. Andreadeli; E. Flemetakis; I. Axarli; M. Dimou; M.K. Udvardi; P. Katinakis; N.E. Labrou ⁎ (pp. 976-984).

Formate dehydrogenases (FDHs, EC 1.2.1.2) comprise a group of enzymes found in both prokaryotes and eukaryotes that catalyse the oxidation of formate to CO₂. FDH1 from the model legume Lotus japonicus ( LjFDH1) was cloned and expressed in E. coli BL21(DE3) as soluble active protein. The enzyme was purified using affinity chromatography on Cibacron blue 3GA-Sepharose. The enzymatic properties of the recombinant enzyme were investigated and the kinetic parameters ( K_m, k_cat) for a number of substrates were determined. Molecular modelling studies were also employed to create a model of LjFDH1, based on the known structure of the Pseudomonas sp. 101 enzyme. The molecular model was used to help interpret biochemical data concerning substrate specificity and catalytic mechanism of the enzyme. The temporal expression pattern of LjFDH1 gene was studied by real-time RT-PCR in various plant organs and during the development of nitrogen-fixing nodules. Furthermore, the spatial transcript accumulation during nodule development and in young seedpods was determined by in situ RNA–RNA hybridization. These results considered together indicate a possible role of formate oxidation by LjFDH1 in plant tissues characterized by relative hypoxia.

Keywords: Abbreviations; PAGE; polyacrylamide gel electrophoresis; SDS; sodium dodecyl sulfate; FDH; formate dehydrogenase,; Lj; FDH1,; Lotus japonicus; FDH1; LjFDH1; cDNA of; Lotus japonicus; FDH1; NAD; ⁺; nicotinamide adenine dinucleotide; NADH; nicotinamide adenine dinucleotide reducedFormate dehydrogenase; Hypoxia; L. japonicus; Nodule; Rhizobium

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BBA - Proteins and Proteomics (v.1794, #6)