Protein-Cofactor Interactions in Bacterial Reaction Centers from Rhodobacter sphaeroides R-26: II. Geometry of the Hydrogen Bonds to the Primary Quinone <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" altimg="si1.gif" display="inline" overflow="scroll"><mml:mrow><mml:msubsup><mml:mtext>Q</mml:mtext><mml:mtext>A</mml:mtext><mml:mrow><mml:mo>⋅</mml:mo><mml:mo></mml:mo><mml:mo>−</mml:mo></mml:mrow></mml:msubsup></mml:mrow></mml:math> by 1H and 2H ENDOR Spectroscopy
Abstract
The geometry of the hydrogen bonds to the two carbonyl oxygens of the semiquinone Q(A)(. -) in the reaction center (RC) from the photosynthetic purple bacterium Rhodobacter sphaeroides R-26 were determined by fitting a spin Hamiltonian to the data derived from (1)H and (2)H ENDOR spectroscopies at 35 GHz and 80 K. The experiments were performed on RCs in which the native Fe(2+) (high spin) was replaced by diamagnetic Zn(2+) to prevent spectral...
Paper Details
Title
Protein-Cofactor Interactions in Bacterial Reaction Centers from Rhodobacter sphaeroides R-26: II. Geometry of the Hydrogen Bonds to the Primary Quinone <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" altimg="si1.gif" display="inline" overflow="scroll"><mml:mrow><mml:msubsup><mml:mtext>Q</mml:mtext><mml:mtext>A</mml:mtext><mml:mrow><mml:mo>⋅</mml:mo><mml:mo></mml:mo><mml:mo>−</mml:mo></mml:mrow></mml:msubsup></mml:mrow></mml:math> by 1H and 2H ENDOR Spectroscopy
Published Date
Jan 1, 2007
Journal
Volume
92
Issue
2
Pages
671 - 682
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