Electron-accepting properties of cytochrome o purified from Vitreoscilla
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چکیده
منابع مشابه
extraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties
آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...
15 صفحه اولBiphasic recombination of photodissociated CO compound of cytochrome o(s) from Vitreoscilla.
The soluble cytochrome o from Vitreoscilla contains two identical subunits and two hemes. The reduced form binds 2 mol of CO in a cooperative manner with a Hill coefficient near 2 (Tyree, B., and Webster, D. A. (1978) J. Biol. Chem. 253, 6988-6991). This carbonyl compound was photolysed with a dye laser and recombination followed at 437 or 420 nm where maximal absorbance changes were registered...
متن کاملPhotodissociation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation.
Oxygenated cytochrome o(s) from Vitreoscilla was photodissociated by a laser flash but the quantum yield was low. The rebinding of oxygen to the ferrous cytochrome proceeded monophasically, and the second order rate constant was 7.8 X 10(7) M-1 s-1, the off rate constant 5.6 X 10(3) s-1, and the calculated dissociation constant for the oxygenated compound 7.2 X 10(-5) M at pH 7.3 and 25 degrees...
متن کاملThe formation of hydrogen peroxide during the oxidation of reduced nicotinamide adenine dinucleotide by cytochrome o from Vitreoscilla.
The formation of hydrogen peroxide during the oxidation of NADH by purified preparations of cytochrome o has been demonstrated by employing three independent methods: polarographic, colorimetric, and fluorometric. The first two methods were used to assay for the accumulation of hydrogen peroxide and showed that hydrogen peroxide did accumulate as a product, but only about 30% of the oxygen cons...
متن کاملProperties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes.
NADPH-cytochrome P-450 reductase has been purified to electrophoretic homogeneity from rabbit liver microsomes by a procedure that may be used in conjunction with the isolation of the major forms of cytochrome P-450. The purified reductase is active in a reconstituted hydroxylation system containingp-45OLM, or P-~~OLM.,. The enzyme contains one molecule each of FMN and FAD per polypeptide chain...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34417-4