Electrostatic properties of cytochrome c variants and of the cytochrome c-cytochrome b5 complex.

1991 ◽  
Vol 43 (2-3) ◽  
pp. 294
Author(s):  
Paul D. Barker ◽  
Marcia R. Mauk ◽  
A.Grant Mauk
Keyword(s):  
Cytochrome C ◽  
Cytochrome B5 ◽  
Electrostatic Properties

Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c

2001 ◽  
Vol 268 (6) ◽  
pp. 1620-1630
Author(s):  
Yibing Wu ◽  
Yunhua Wang ◽  
Chengmin Qian ◽  
Jun Lu ◽  
Ercheng Li ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Solution Structure ◽  
Cytochrome B5

Use of specific trifluoroacetylation of lysine residues in cytochrome c to study the reaction with cytochrome b5, cytochrome c1, and cytochrome oxidase

1980 ◽  
Vol 592 (2) ◽  
pp. 303-313 ◽  
Author(s):  
Michael B. Smith ◽  
Jacqueline Stonehuerner ◽  
Aftab J. Ahmed ◽  
Nicole Staudenmayer ◽  
Francis Millett
Keyword(s):  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Cytochrome B5 ◽  
Cytochrome C1 ◽  
Lysine Residues

scholarly journals Electron-transport pathway of the NADH-dependent haem oxygenase system of rat liver microsomal fraction induced by cobalt chloride

1979 ◽  
Vol 178 (2) ◽  
pp. 323-329 ◽  
Author(s):  
Y Hino ◽  
S Minakami
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Microsomal Fraction ◽  
Cytochrome B5 ◽  
Transport Pathway ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Haem Oxygenase ◽  
Reported Data ◽  
Nadph Cytochrome C Reductase

The hepatic microsomal haem oxygenase activity of rats treated with CoCl2 was studied kinetically by measuring biliverdin, the immediate product of the reaction. Biliverdin was extracted with diethyl ether/ethanol mixture, and was determined by the difference between A690 and A800. The apparent Km value for NADPH (at 50 microM-haematin) was about 0.2 microM when an NADPH-generating system was used, whereas that for NADH was about 630 microM. Essentially the same Vmax. values were obtained for both the NADH- and NADPH-dependent haem oxygenase reactions. No synergism was observed with NADH and NADPH. The NADH-dependent reaction was competitively inhibited by NADP+, with a Ki of about 10 microM. The inhibitoin of the NADH-dependent reaction by the antibody against rat liver microsomal NADPH-cytochrome c reductase was essentially complete, with a pattern similar to that of the NADPH-dependent reaction. The immunochemical experiment and the comparison of the kinetic values with the reported data on isolated NADH-cytochrome b5 reductase and NADPH–cytochrome c reductase indicated the involvement of the latter enzyme in NADH-dependent haem oxygenation by microsomal fraction in situ.

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