NDLI: Reorientation of cytochrome c<sub>2</sub> upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer

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Reorientation of cytochrome c₂ upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer

Control of the stereo-selectivity of styrene epoxidation by cytochrome P450 BM3 using structure-based mutagenesis

Circular dichroism spectra of cytochrome c oxidase

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Metallomics Vol - 3 Issue - 3

Metallomics Vol - 3 Issue - 2

Metallomics Vol -2

Metallomics Vol -1

Reorientation of cytochrome c₂ upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer

Content Provider	Royal Society of Chemistry (RSC)
Author	Osyczka, Artur Pietras, Rafał Froncisz, Wojciech Sarewicz, Marcin
Copyright Year	2011
Abstract	The reaction of water-soluble cytochrome c (c2) with its physiological redox partners is facilitated by electrostatic attractions between the two protein surfaces. Using spin-labeled cytochrome c2 from Rhodobacter capsulatus and pulse electron paramagnetic resonance (EPR) measurements we compared spatial orientation of cytochrome c2 upon its binding to surfaces of opposite charge. We observed that cytochrome c2 can use its negatively charged “back” side when exposed to interact with positively charged surfaces (DEAE resin) which is the opposite to the use of its positively charged “front” side in physiological interaction with negatively charged binding domain of cytochromebc1. The later orientation is also adopted upon non-physiological binding of cytochrome c2 to negatively charged carboxymethyl cellulose resin. These results directly demonstrate how the electric dipolar nature of cytochrome c2 influences its orientation in interactions with charged surfaces, which may facilitate collisions with other redox proteins in a proper orientation to support physiologically-competent electron transfer. Saturation recovery EPR provides an attractive tool for monitoring spatial orientation of proteins in their interaction with surfaces in liquid phase. It is particularly valuable for metalloproteins engaged in redox reactions as a means to monitor the geometry and dynamics of formation of protein complexes in measurements that are independent of electron transfer processes.
Starting Page	404
Ending Page	409
Page Count	6
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	3
Issue Number	4
Journal	Metallomics
DOI	10.1039/c0mt00105h
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Carboxymethyl cellulose Rhodobacter capsulatus Spin label EPR Interaction Redox Electron paramagnetic resonance Protein Ion-exchange resin Molecular geometry
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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Redox-related conformational changes in Rhodobacter capsulatus cytochrome c2.

Cytochrome c2-independent respiratory growth of Rhodobacter capsulatus.

Redox-related conformational changes in Rhodobacter capsulatus cytochrome c2.

Identification of nitric oxide reductase activity in Rhodobacter capsulatus: the electron transport pathway can either use or bypass both cytochrome c2 and the cytochrome bc1 complex.

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The cytochrome bc1 complex of Rhodobacter sphaeroides can restore cytochrome c2-independent photosynthetic growth to a Rhodobacter capsulatus mutant lacking cytochrome bc1.

Interactive control of rhodobacter capsulatus redox-balancing systems during phototrophic metabolism (2001).

Complex i and its involvement in redox homeostasis and carbon and nitrogen metabolism in rhodobacter capsulatus (2001).

Cytochrome c - from rhodobacter capsulatus confers increased resistance to nitric oxide (1999).

Reorientation of cytochrome c₂ upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer

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Reorientation of cytochrome c2 upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer

Reorientation of cytochrome c₂ upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer