Reactivity of photoreduced cytochrome aa3 complexes with molecular oxygen
نویسندگان
چکیده
منابع مشابه
Cytochrome aa3 from Nitrosomonas europaea.
Cytochrome c oxidase has been purified from the ammonia oxidizing chemoautotroph Nitrosomonas europaea by ion-exchange chromatography in the presence of Triton X-100. The enzyme has absorption maxima at 420 and 592 nm in the resting state and at 444 and 598 nm in the dithionite-reduced form; optical extinction coefficient (598 nm minus 640 nm) = 21.9 cm-1 nM-1. The enzyme has approximately 11 n...
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Uncharged reductants, such as NNN'N'-tetramethyl-p-phenylenediamine and diaminodurene, reduce cytochrome c at both high and low ionic strength, unlike ascorbate, which is effective only at low ionic strength. The 'tightly bound' cytochrome c-cytochrome c oxidase complex, with 1 equiv. of cytochrome c per cytochrome aa3, can be prepared by simple mixing of the two component species. Its properti...
متن کاملMultiwavelength analysis of the kinetics of reduction of cytochrome aa3 by cytochrome c.
Some new approaches to the kinetic study of the reduction of cytochrome aa3 by cytochrome c are presented. The primary innovations are the use of a spectrometer which can acquire multiwavelength data as fast as every 10 microseconds, and the application of a variety of analytical methods which can utilize simultaneously all of the time-resolved spectral data. These techniques include singular v...
متن کاملHigh-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes.
When grown in aerated shaking culture, Bacillus subtilis expresses two different haem A-containing terminal oxidases: cytochrome aa3-quinol oxidase and cytochrome caa3 oxidase. This paper describes a high-yield conventional procedure for purifying the two haem A-containing oxidases from the same aerobic culture of Bacillus subtilis. Yields of close to 40% of the total haem A are achieved and ab...
متن کاملMetalloprotein electron transfer reactions: analysis of reactivity of horse heart cytochrome c with inorganic complexes.
The reactions of horse heart cytochrome c with Fe(ethylenediaminetetraacetate)2-, Co(1,10-phenanthroline)3(3+), Ru(NH3)6(2+), and Fe(CN)6(3-) have been analyzed within the formalism of the Marcus theory of outer-sphere electron transfer, including compensation for electrostatic interactions. Calculated protein self-exchange rate constants based on crossreactions are found to vary over three ord...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1981
ISSN: 0264-6021
DOI: 10.1042/bj1940713