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pH Dependence of Ferricytochrome c Conformational Transitions during Binding to Cardiolipin Membranes: Evidence for Histidine as the Distal Ligand at Neutral pH
Journal article   Peer reviewed

pH Dependence of Ferricytochrome c Conformational Transitions during Binding to Cardiolipin Membranes: Evidence for Histidine as the Distal Ligand at Neutral pH

Bridget Milorey, Dmitry Malyshka and Reinhard Schweitzer-Stenner
The journal of physical chemistry letters, v 8(9), pp 1993-1998
04 May 2017
PMID: 28418677

Abstract

Chemistry Chemistry, Physical Materials Science Materials Science, Multidisciplinary Nanoscience & Nanotechnology Physical Sciences Physics Physics, Atomic, Molecular & Chemical Science & Technology Science & Technology - Other Topics Technology
The conformational changes of ferricytochrome c upon binding to cardiolipin-containing small unilamellar vesicles were studied at slightly acidic pH using fluorescence, visible circular dichroism, UV-visible absorption, and resonance Raman spectroscopy. The obtained spectroscopic response data suggest a mode of interaction, which is clearly distinct from the binding process observed at neutral pH. Evidence of a reversible and electrostatic binding mechanism under these conditions is provided through binding inhibition in the presence of 150 mM NaCl. Moreover, UV-visible absorption and resonance Raman spectra reveal that the conformational ensemble of membrane bound cytochrome c is dominated by a mixture of conformers with pentacoordinated and hexacoordinated high-spin heme irons, which contrast with the dominance of low-spin species at neutral pH. While our results confirm the L-site binding proposed by Kawai et al., they point to the protonation of a histidine ligand (H33) as conformational trigger.

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Chemistry, Physical
Materials Science, Multidisciplinary
Nanoscience & Nanotechnology
Physics, Atomic, Molecular & Chemical
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