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Structural and mechanistic mapping of a unique fumarate reductase.

Taylor P, Pealing SL, Reid GA, Chapman SK, Walkinshaw MD
Nat Struct Biol 6 1108-12 (1999)
Cited: 81 times
EuropePMC logo PMID: 10581550

Abstract

The 1.8 A resolution crystal structure of the tetraheme flavocytochrome c3, Fcc3, provides the first mechanistic insight into respiratory fumarate reductases or succinate dehydrogenases. The multi-redox center, three-domain protein shows a 40 A long 'molecular wire' allowing rapid conduction of electrons through a new type of cytochrome domain onto the active site flavin, driving the reduction of fumarate to succinate. In this structure a malate-like molecule is trapped in the enzyme active site. The interactions between this molecule and the enzyme suggest a clear mechanism for fumarate reduction in which the substrate is polarized and twisted, facilitating hydride transfer from the reduced flavin and subsequent proton transfer. The enzyme active site in the oxidized form is completely buried at the interface between the flavin-binding and the clamp domains. Movement of the cytochrome and clamp domains is postulated to allow release of the product.

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  1. Multi-haem cytochromes in Shewanella oneidensis MR-1: structures, functions and opportunities. Breuer M, Rosso KM, Blumberger J, Butt JN. J R Soc Interface 12 20141117 (2015)
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