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Changes induced by hydrazine in optical spectra of cytochrome oxidase
Author(s) -
Markossian Kira A.,
Paitian Norair A.,
Nalbandyan Robert M.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80503-1
Subject(s) - hydrazine (antidepressant) , electron paramagnetic resonance , chemistry , cytochrome c oxidase , oxidase test , photochemistry , oxygen , spectral line , anaerobic exercise , cytochrome , enzyme , inorganic chemistry , stereochemistry , nuclear magnetic resonance , biochemistry , organic chemistry , biology , physics , astronomy , physiology
Under aerobic conditions hydrazine reduces haem a of cardiac cytochrome oxidase and brings about the formation in optical spectra of a new band at 845 nm, whereas under anaerobic conditions hydrazine reduces both haems, a and a 3 , as well as EPR‐detectable copper, Cu A , and results in the band at 845 nm. The formation of this band was sensitive to inhibitors of oxygen binding. It is suggested that the band at 845 nm reflects changes induced by hydrazine in Cu B which in the resting enzyme is EPR‐undetectable.