Synthesis and Physical Characterization of Novel Heme-Based Model Systems for Photoinitiated Electron Transfer. 1. Complexation of a RuProHis Bifunctional Peptide and Microperoxidase-11

Autor:	M. C. Simpson, T. Niemczyk, D. L. Fontenot, Randy W. Larsen, S. Zhang, John A. Shelnutt, Mark R. Ondrias, S. Niu, L. Martinez, R. Falcon, B. Fan
Rok vydání:	1997
Předmět:	Dipeptide chemistry.chemical_element Photochemistry Ruthenium Inorganic Chemistry Electron transfer Bipyridine chemistry.chemical_compound symbols.namesake chemistry symbols Moiety Physical and Theoretical Chemistry Bifunctional Raman spectroscopy Heme
Zdroj:	Inorganic Chemistry. 36:3839-3846
ISSN:	1520-510X 0020-1669
Popis:	This paper describes the synthesis and initial physical characterization of a new type of model system for the investigation of photoinitiated electron transfer (ET) in proteins and polypeptides. This system is based upon a derivative of a heme-containing digestion product of cytochrome c, microperoxidase-11 (MP-11). The vacant axial position of the five-coordinate heme of MP-11 is coordinated to the terminal histidine of a dipeptide having a photoactive ruthenium tris(bipyridine) moiety at its other end (RuProHis). Photoexcitation of the ruthenium group results in rapid (kET > 10 7 s -1 ), reversible ET to the ferric heme. The equilibrium properties of MP-11 and the MP-11/Ru(peptide) complex were characterized with optical absorption, luminescence, and resonance Raman (RR) spectroscopies. Molecular modeling was also employed to examine the structure and energetics of the equilibrium species. Clear evidence for reversible photoinduced ET was observed in time-resolved luminescence and transient resonance Raman studies of the MP-11/RuProHis samples.
Databáze:	OpenAIRE
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