Nitric oxide and the respiratory enzyme.
Available information on the molecular mechanisms by which nitric oxide (NO) controls the activity of the respiratory enzyme (cytochrome-c-oxidase) is reviewed. We report that, depending on absolute electron flux, NO at physiological concentrations reversibly inhibits cytochrome-c-oxidase by two alternative reaction pathways, yielding either a nitrosyl- or a nitrite-heme a3 derivative. We address a number of hypotheses, envisaging physiological and/or pathological effects of the reactions between NO and cytochrome-c-oxidase.
Brunori
Maurizio
M
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, I-00185 Rome, Italy. maurizio.brunori@uniroma1.it
Forte
Elena
E
Arese
Marzia
M
Mastronicola
Daniela
D
Giuffrè
Alessandro
A
Sarti
Paolo
P
D000818:Animals; D019069:Cell Respiration / Q000187:drug effects; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D009569:Nitric Oxide / Q000378:metabolism* / Q000494:pharmacology; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism
D008024:Ligands; D009569:Nitric Oxide; D003576:Electron Transport Complex IV; D010100:Oxygen