Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up.

Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Research Abstract Details 

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Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Abstract Text:

Jing Hong,Olesya A Kharenko,Michael Y Ogawa,

The alpha-helical coiled-coil motif serves as a robust scaffold for incorporating electron-transfer (ET) functionality into synthetic metalloproteins. These structures consist of a supercoiling of two or more aplha helices that are formed by the self-assembly of individual polypeptide chains whose sequences contain a repeating pattern of hydrophobic and hydrophilic residues. Early work from our group attached abiotic Ru-based redox sites to the most surface-exposed positions of two stranded coiled-coils and used electron-pulse radiolysis to study both intra- and intermolecular ET reactions in these systems. Later work used smaller metallopeptides to investigate the effects of conformational gating within electrostatic peptide-protein complexes. We have recently designed the C16C19-GGY peptide, which contains Cys residues located at both the "a" and "d" positions of its third heptad repeat in order to construct a nativelike metal-binding domain within its hydrophobic core. It was shown that the binding of both Cd(II) and Cu(I) ions induces the peptide to undergo a conformational change from a disordered random coil to a metal-bridged coiled-coil. However, whereas the Cd(II)-protein exists as a two-stranded coiled-coil, the Cu(I) derivative exists as a four-stranded coiled-coil. Upon the incorporation of other metal ions, metal-bridged peptide dimers, tetramers, and hexamers are formed. The Cu(I)-protein is of particular interest because it exhibits a long-lived (microsecond) room-temperature luminescence at 600 nm. The luminophore in this protein is thought to be a multinuclear CuI4Cys4(N/O)4 cage complex, which can be quenched by exogenous electron acceptors in solution, as shown by emission-lifetime and transient-absorption experiments. It is anticipated that further investigation into these systems will contribute to the expanding effort of bioinorganic chemists to prepare new kinds of functionally active synthetic metalloproteins.

Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Publishing Authors By Initials

J Hong,OA Kharenko,MY Ogawa,

For similar natural sciences: chemistry: chemistry, physical: viscosity research abstracts see: natural sciences: chemistry: chemistry, physical: viscosity research

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Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Inorganic chemistry

VOLUME: 45

Page Numbers: 9974-84

Journal Abbreviation:

ISSN: 0020-1669

DAY: 11

MONTH: Dec

YEAR: 2006

Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 366543

Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Keywords Mesh Terms:

KEYWORDS: Viscosity

MESH TERMS: chemistry

Chemical & Substance for Abstract: Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up. Information

Substance Name: Copper

Registry Number: 7440-50-8

Grant and Affiliation Information for Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up.

AFFILIATION: Department of Chemistry and Center for Photochemical Sciences, Bowling Green State University, Bowling Green, Ohio 43403, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM61171

ACRONYM: GM

MEDLINETA: Inorg Chem

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