Studies on the microsomal electron-transport system of anaerobically grown yeast. IV. Purification and characterization of NADH-cytochrome b5 reductase.

Abstract:

:The presence of NADH-cytochrome b5 reductase [EC 1.6.2.2] in microsomes from anaerobically grown yeast was confirmed by its isolation and purification. The purified preparation of the reductase showed an apparent molecular weight of 27,000 daltons. The reductase appeared to contain loosely-bound FAD as a prosthetic group. The reductase required NADH as a specific electron donor, and could reduce some redox dyes as well as cytochrom b5. The reductase, however, could not reduce cytochrome c. Michaelis constants of the reductase for NADH and calf liver cytochrome b5 were 6.3 and 1.5 micron M, respectively, and optimal pH for cytochrome b5 reduction was 5.6. Although some differences exist between the properties of NADH-cytochrome b5 reductase from yeast and from mammalia, the results indicate a functional similarity of the present enzyme to mammalian NADH-cytochrome b5 reductase in the microsomal electron-transport system.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kubota S,Yoshida Y,Kumaoka H

doi

10.1093/oxfordjournals.jbchem.a131434

keywords:

subject

Has Abstract

pub_date

1977-01-01 00:00:00

pages

187-95

issue

1

eissn

0021-924X

issn

1756-2651

journal_volume

81

pub_type

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