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BBA - Bioenergetics (v.1707, #1)

Editorial Board (pp. ii).
Preface (pp. vi-vii).

Reaction of haem containing proteins and enzymes with hydroperoxides: The radical view by Dimitri A. Svistunenko (pp. 127-155).
The reaction between hydroperoxides and the haem group of proteins and enzymes is important for the function of many enzymes but has also been implicated in a number of pathological conditions where oxygen binding proteins interact with hydrogen peroxide or other peroxides. The haem group in the oxidized Fe3+ (ferric) state reacts with hydroperoxides with a formation of the Fe4+=O (oxoferryl) haem state and a free radical primarily located on the π-system of the haem. The radical is then transferred to an amino acid residue of the protein and undergoes further transfer and transformation processes. The free radicals formed in this reaction are reviewed for a number of proteins and enzymes. Their previously published EPR spectra are analysed in a comparative way. The radicals directly detected in most systems are tyrosyl radicals and the peroxyl radicals formed on tryptophan and possibly cysteine. The locations of the radicals in the proteins have been reported as follows: Tyr133 in soybean leghaemoglobin; αTyr42, αTrp14, βTrp15, βCys93, (αTyr24−αHis20), all in the α- and β-subunits of human haemoglobin; Tyr103, Tyr151 and Trp14 in sperm whale myoglobin; Tyr103, Tyr146 and Trp14 in horse myoglobin; Trp14, Tyr103 and Cys110 in human Mb. The sequence of events leading to radical formation, transformation and transfer, both intra- and intermolecularly, is considered. The free radicals induced by peroxides in the enzymes are reviewed. Those include: lignin peroxidase, cytochrome c peroxidase, cytochrome c oxidase, turnip isoperoxidase 7, bovine catalase, two isoforms of prostaglandin H synthase, Mycobacterium tuberculosis and Synechocystis PCC6803 catalase-peroxidases.

Keywords: Abbreviations; AA; arachidonic acid; apo; prefix for the haem proteins that are forced to lose their haem group; BLC; bovine liver catalase; C; c; O; cytochrome; c; oxidase; C; c; P; cytochrome; c; peroxidase; CuOOH; cumene hydroperoxide PhC(CH; 3; ); 2; OOH; Cyt; c; cytochrome; c; DBNBS; 3,5-dibromo-4-nitrosobenzenesulfonic acid; DMPO; 5,5-dimethyl-1-pyrroline; N; -oxide; EPR; electron paramagnetic resonance; EtOOH; ethyl hydroperoxide,C; 2; H; 5; OOH; FAD; flavin adenine dinucleotide; Hb; haemoglobin; HbA; human haemoglobin; HF; high frequency/high field (EPR spectroscopy); HH; horse heart (myoglobin); HRP; horseradish peroxidase; h.s.; high spin; HSM; horse skeletal muscle; IS; ‘inhibited singlet’ (in PGHS); Lb; leghaemoglobin; l.s.; low spin; Mb; myoglobin; met; prefix for the haem proteins in the oxidized Fe; 3+; state; MLC; Micrococcus luteus; (; lysodeikticus; ) catalase; MNP; 2-ethyl-2-nitrosopropane; NS; narrow singlet (a PGHS EPR signal); PAA; peroxyacetic acid CH; 3; C(O)OOH; PDB; Protein data Bank; PG; prostaglandin; PGHS; prostaglandin H synthase; PMC; Proteus mirabilis; catalase; PRRAD; Phenol Ring Rotation Angle Database; oxy; prefix for the haem proteins in the reduced and oxygenated state Fe; 2+; –O; 2; SW; sperm whale; tBuOOH; tert; -butyl hydroperoxide, C; 4; H; 9; OOH; TIP; turnip isoperoxidase; TRSSA; Tyrosyl Radical Spectra Simulation Algorithm; WD; wide doublet (a PGHS EPR signal); WS; wide singlet (in PGHS)Haem; Heme; Peroxide; Tyrosine; Tryptophan; Cysteine; Radical
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