[A study of the interaction of substrates with cytochrome P-450 by a method of UV- and 1H-NMR spectroscopy].
Acceleration of substrate longitudinal relaxation (T1) was used to study cytochrome P-450-aminopyrine (1st type substrate) and P-450-4-methoxypyridine (2nd type substrate) complexes. Dissociation constant, T1 and/or residence time of substrate in the complex can be obtained from the dependence of T1 of substrate protons on substrate concentration. Basing on the relaxation times, distances between Fe3+ ion in the active site and protons of the substrate moiety were determined. For aminopyrine all the distances proved to be about 8 A. In the P-450-4-methoxypyridine complex the pyridine nitrogen is directed towards Fe3+ ion. Cytochrome P-450 is compared with its denatured form, cytochrome P-420, and metmyoglobin.
Vol'dman
Iu Iu
IuIu
Guliaeva
L F
LF
Vaĭner
L M
LM
Liakhovich
V V
VV
D000632:Aminopyrine / Q000378:metabolism; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D003580:Cytochromes / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D009211:Myoglobin / Q000378:metabolism; D011725:Pyridines / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D003580:Cytochromes; D009211:Myoglobin; D011725:Pyridines; D000632:Aminopyrine; C051376:4-methoxypyridine; C013464:cytochrome P420; D003577:Cytochrome P-450 Enzyme System
Izuchenie vzaimodeĭstviia substratov s tsitokhromom P-450 metodom UF- i 1H-IaMR-spektroskopii.