Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1787, Issue 2, Pages 113-120Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2008.11.007
Keywords
Respiratory enzyme; Fumarate; Heme; NMR; Redox; Electrostatic interaction
Categories
Funding
- Fundacao para a Ciencia e a Tecnologia (Portugal) [PPCDT/BIA-PRO/58722/2004, POCI/QUI/58985/2004, POCI/QUI/60060/2004, PPCDT/QUI/60060/2004]
- FCT, Portugal [SFRH/5229/2001]
- Fundação para a Ciência e a Tecnologia [POCI/QUI/58985/2004, POCI/QUI/60060/2004] Funding Source: FCT
Ask authors/readers for more resources
The fumarate reductases from S. frigidimarina NCIMB400 and S. oneidensis MR-1 are soluble and monomeric enzymes located in the periplasm of these bacteria. These proteins display two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site. This arrangement of single-electron redox co-factors leading to multiple-electron active sites is widespread in respiratory enzymes. To investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multi-electron catalytic site, redox titrations followed by NMR and visible spectroscopies were applied to determine the microscopic thermodynamic parameters of the hemes. The results show that the redox behaviour of these fumarate reductases is similar and 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. (C) 2008 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available