@article {6233,
	title = {Structure of a novel dodecaheme cytochrome c from Geobacter sulfurreducens reveals an extended 12 nm protein with interacting hemes},
	journal = {Journal of Structural Biology},
	volume = {174},
	year = {2011},
	pages = {223-233},
	abstract = {<p>Multiheme cytochromes c are important in electron transfer pathways in reduction of both soluble and insoluble Fe(III) by Geobacter sulfurreducens. We determined the crystal structure at 3.2 {\r A} resolution of the first dodecaheme cytochrome c (GSU1996) along with its N-terminal and C-terminal hexaheme fragments at 2.6 and 2.15 {\r A} resolution, respectively. The macroscopic reduction potentials of the full-length protein and its fragments were measured. The sequence of GSU1996 can be divided into four c7-type domains (A, B, C and D) with homology to triheme cytochromes c7. In cytochromes c7 all three hemes are bis{\textendash}His coordinated, whereas in c7-type domains the last heme is His{\textendash}Met coordinated. The full-length GSU1996 has a 12 nm long crescent shaped structure with the 12 hemes arranged along a polypeptide to form a {\textquotedblleft}nanowire{\textquotedblright} of hemes; it has a modular structure. Surprisingly, while the C-terminal half of the protein consists of two separate c7-type domains (C and D) connected by a small linker, the N-terminal half of the protein has two c7-type domains (A and B) that form one structural unit. This is also observed in the AB fragment. There is an unexpected interaction between the hemes at the interface of domains A and B, which form a heme-pair with nearly parallel stacking of their porphyrin rings. The hemes adjacent to each other throughout the protein are within van der Waals distance which enables efficient electron exchange between them. For the first time, the structural details of c7-type domains from one multiheme protein were compared.</p>
},
	url = {http://www.sciencedirect.com/science/article/pii/S104784771000359X},
	author = {Pokkuluri, P.R. and Londer, Yuri Y. and Norma E.C. Duke and Miguel Pessanha and Yang, X. and Orshonsky, V. and L. Orshonsky and Erickson, J. and Y. Zagyanskiy and Salgueiro, C.A. and Schiffer, M.}
}
