Design of dinuclear manganese cofactors for bacterial reaction centers

Olson, Tien L., Espiritu, Eduardo, Edwardraja, Selvakumar, Simmons, Chad R., Williams, JoAnn C., Ghirlanda, Giovanna and Allen, James P. (2016) Design of dinuclear manganese cofactors for bacterial reaction centers. Biochimica et Biophysica Acta - Bioenergetics, 1857 5: 539-547. doi:10.1016/j.bbabio.2015.09.003

Author Olson, Tien L.
Espiritu, Eduardo
Edwardraja, Selvakumar
Simmons, Chad R.
Williams, JoAnn C.
Ghirlanda, Giovanna
Allen, James P.
Title Design of dinuclear manganese cofactors for bacterial reaction centers
Journal name Biochimica et Biophysica Acta - Bioenergetics   Check publisher's open access policy
ISSN 0005-2728
Publication date 2016-05-01
Year available 2016
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1016/j.bbabio.2015.09.003
Open Access Status Not yet assessed
Volume 1857
Issue 5
Start page 539
End page 547
Total pages 9
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Formatted abstract
A compelling target for the design of electron transfer proteins with novel cofactors is to create a model for the oxygen-evolving complex, a Mn4Ca cluster, of photosystem II. A mononuclear Mn cofactor can be added to the bacterial reaction center, but the addition of multiple metal centers is constrained by the native protein architecture. Alternatively, metal centers can be incorporated into artificial proteins. Designs for the addition of dinuclear metal centers to four-helix bundles resulted in three artificial proteins with ligands for one, two, or three dinuclear metal centers able to bind Mn. The three-dimensional structure determined by X-ray crystallography of one of the Mn-proteins confirmed the design features and revealed details concerning coordination of the Mn center. Electron transfer between these artificial Mn-proteins and bacterial reaction centers was investigated using optical spectroscopy. After formation of a light-induced, charge-separated state, the experiments showed that the Mn-proteins can donate an electron to the oxidized bacteriochlorophyll dimer of modified reaction centers, with the Mn-proteins having additional metal centers being more effective at this electron transfer reaction. Modeling of the structure of the Mn-protein docked to the reaction center showed that the artificial protein likely binds on the periplasmic surface similarly to cytochrome c2, the natural secondary donor. Combining reaction centers with exogenous artificial proteins provides the opportunity to create ligands and investigate the influence of inhomogeneous protein environments on multinuclear redox-active metal centers. This article is part of a Special Issue entitled Biodesign for Bioenergetics — the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.
Keyword De novo protein design
Electron transfer
Four-helix bundles
Mn-binding proteins
Photosystem II
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID CHE 1505874
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 4 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 21 Apr 2017, 11:39:19 EST by Selvakumar Edwardraja on behalf of Learning and Research Services (UQ Library)