Identification of a cysteine involved in the interaction between carbon monoxide dehydrogenase and corrinoid/Fe-S protein from Clostridium thermoaceticum.

Abstract:

:In Clostridium thermoaceticum, the synthesis of acetyl-CoA from methyl tetrahydrofolate occurs via a series of enzymatic reactions involving methyl transferase, corrinoid/Fe-S protein (corrinoid), carbon monoxide dehydrogenase (CODH) and ferredoxin. We have investigated the possibility of one or more of these proteins existing as multi-enzyme complexes in vivo with higher catalytic activity. A protein complex consisting of CODH and corrinoid was isolated from the cell-free extracts of Clostridium thermoaceticum. The acetyl-CoA synthesis was found to be approximately 1.8-fold higher with the complex than that observed with the isolated protein components. HPLC gel filtration analyses of the native and DTE reduced complex suggested that the CODH:corrinoid complex is held together primarily by an inter disulfide bond. By differential labeling of thiols with [14C]N-ethylmaleimide it was found that Cys-506 of the alpha subunit of CODH was involved in the disulfide linkage with the corrinoid of the complex.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Shanmugasundaram T,Sundaresh CS,Kumar GK

doi

10.1016/0014-5793(93)81808-d

subject

Has Abstract

pub_date

1993-07-12 00:00:00

pages

281-4

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)81808-D

journal_volume

326

pub_type

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