NDLI: Ab initio structure solution of a dimeric cytochrome c 3 from Desulfovibrio gigas containing disulfide bridges

Content Provider	Springer Nature Link
Author	Frazão, Carlos Sieker, Larry Sheldrick, George Lamzin, Victor LeGall, Jean Carrondo, M. A.
Copyright Year	1999
Abstract	The 1.2 Å resolution crystal structure of the 29 kDa di-tetrahaem cytochrome c 3 from the sulfate reducing bacterium Desulfovibrio gigas was solved by ab initio methods, making this the largest molecule to be solved by this procedure. The actual refined model of the cysteine-linked dimeric molecule reveals that this molecule is very similar to the non-covalently linked symmetrical dimer of the di-tetrahaem cytochrome c 3 from Desulfomicrobium norvegicum. Each monomer has the typical polypeptide fold, haem arrangement and iron coordination found for the tetrahaem cytochrome c 3 molecules. The interface between the covalently linked monomers in the asymmetric unit of the crystal shows a pseudo two-fold arrangement, disturbed from symmetry by crystal packing forces. The fact that D. gigas contains a dimeric tetrahaem cytochrome with solvent accessible disulfide bridges and that this cytochrome specifically couples hydrogen oxidation to thiosulfate reduction in bacterial extracts provides an interesting aspect related to disulfide exchange reactions in this microorganism.
Starting Page	162
Ending Page	165
Page Count	4
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	4
Issue Number	2
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	1999-05-05
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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