Nicotinamide adenine dinucleotide -- independent formate dehydrogenase in Mycobacterium phlei.

Abstract:

:Formate dehydrogenase activity (EC 1.2.1.2) has been demonstrated in cell-free preparations of Mycobacterium phlei by following the reduction of 2,6 dichlorophenolindophenol. thiazolyl blue tetrazolium, or equine cytochrome c. The reduction of equine cytochrome c was inhibited by 2-heptyl-4-hydroxyquinoline-N-oxide. Neither nicotinamide adenine dinucleotide nor nicotinamide adenine dinucleotide phosphate were reduced by this formate dehydrogenase. The enzyme was constitutive and associated with the particular fraction. The greatest level of activity was observed at pH 9.0, with 8 mM formate, and with extracts of cells taken from the log phase of growth. Formaldehyde, hypophosphite, nitrate, and bicarbonate all inhibited the oxidation of formate.

journal_name

Can J Microbiol

authors

Deyhle RR,Barton LL

doi

10.1139/m77-018

subject

Has Abstract

pub_date

1977-02-01 00:00:00

pages

125-30

issue

2

eissn

0008-4166

issn

1480-3275

journal_volume

23

pub_type

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