Isolation and some properties of NAD+ reductase of the green photosynthetic bacterium Prosthecochloris aestuarii.

Abstract:

:NAD+ reductase of the green photosynthetic bacterium Prosthecochloris aestuarii was isolated and purified by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and Sephadex G-200 gel filtration. This enzyme is an FAD-containing flavoprotein and has absorption maxima at 485 (shoulder0 452, 411, and 385 nm (the 411 nm band is due to cytochrome). The molecular weight of the enzyme as determined by gel filtration using Sephadex G-200 is 119,000. The enzyme catalyzes the reduction of NAD+ and NADP+ by photoreduced spinach ferredoxin or reduced benzyl viologen...

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Shioi Y,Takamiya K,Nishimura M

doi

10.1093/oxfordjournals.jbchem.a131079

subject

Has Abstract

pub_date

1976-02-01 00:00:00

pages

361-71

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

79

pub_type

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