PROTEIN COMPLEXES INVOLVED IN ELECTRON TRANSFER AND BACTERIAL CHEMOTAXIS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We aim to understand the structural basis for long-range electron transfer(ET) in biology. The vast number of conformational and chemical states available to the polypeptide chain allows nature to tune the reactivity of metal centers and direct electron flow within and between proteins. We have developed and applied new photochemical methods for studying ET in single protein crystals, where structure can be precisely defined by X-ray crystallography. Designed crystal systems that fix donor and acceptor orientation allow effects of intervening protein and water structure on ET to be probed by combining rate measurements in the crystals with high-resolution structure determinations. ET rates are currently being determined directly in crystals of complexes between cytochrome c peroxidase (CcP) and cytochrome c (Cc).