Literature summary for 1.3.5.1 extracted from

Pessanha, M.; Rothery, E.L.; Miles, C.S.; Reid, G.A.; Chapman, S.K.; Louro, R.O.; Turner, D.L.; Salgueiro, C.A.; Xavier, A.V.
Tuning of functional heme reduction potentials in Shewanella fumarate reductases (2009), Biochim. Biophys. Acta, 1787, 113-120.

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Organism

Organism	UniProt	Comment	Textmining
Shewanella frigidimarina	-	NCIMB400	-
Shewanella frigidimarina NCIMB400	-	NCIMB400	-
Shewanella oneidensis	-	MR-1	-
Shewanella oneidensis MR-1 / ATCC 700550	-	MR-1	-

Synonyms

Synonyms	Comment	Organism
fumarate reductase	-	Shewanella oneidensis
fumarate reductase	-	Shewanella frigidimarina

Cofactor

Cofactor	Comment	Organism	Structure
FAD	proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV	Shewanella oneidensis
FAD	proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV	Shewanella frigidimarina
heme	proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV	Shewanella oneidensis
heme	proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV	Shewanella frigidimarina

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Release 2023.1 (January 2023)