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Voltammetric studies of bidirectional catalytic electron transport in Escherichia coli succinate dehydrogenase: comparison with the enzyme from beef heart mitochondria.

Abstract:

The succinate dehydrogenases (SDH: soluble, membrane-extrinsic subunits of succinate:quinone oxidoreductases) from Escherichia coli and beef heart mitochondria each adsorb at a pyrolytic graphite 'edge' electrode and catalyse the interconversion of succinate and fumarate according to the electrochemical potential that is applied. E. coli and beef heart mitochondrial SDH share only ca. 50% homology, yet the steady-state catalytic activities, when measured over a continuous potential range, dis...

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Publication status:
Published

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
Journal:
Biochimica et biophysica acta More from this journal
Volume:
1412
Issue:
3
Pages:
262-272
Publication date:
1999-08-01
DOI:
ISSN:
0006-3002
Language:
English
Keywords:
Pubs id:
pubs:31549
UUID:
uuid:f9d9539a-3f6b-4353-9127-833c2482072d
Local pid:
pubs:31549
Source identifiers:
31549
Deposit date:
2013-11-16

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