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Identification of histidine as an axial ligand to P700+.
Mac, M; Tang, X S; Diner, B A; McCracken, J; Babcock, G T.
Afiliação
  • Mac M; Department of Chemistry, Michigan State University, East Lansing 48824, USA.
Biochemistry ; 35(41): 13288-93, 1996 Oct 15.
Article em En | MEDLINE | ID: mdl-8873594
ABSTRACT
The primary electron donor in photosystem I (PSI), P700, is thought to be a dimeric Chl a species. Neither the electronic nor geometric structure of the cation radical is clearly understood. Magnetic resonance studies have indicated that the unpaired electron in P700+ is delocalized asymmetrically over the Chl dimer; however, the axial ligand to the central Mg2+ is not known. The recent development of a histidine tolerant mutant of Synechocystis PCC 6803 has allowed us to use a combination of isotopic labeling and electron nuclear double resonance (ENDOR) spectroscopy to show the first definitive spectroscopic evidence of a histidine ligand to P700+. Peaks split symmetrically about the 15N Larmor frequency corresponding to an isotropic hyperfine coupling of 0.64 MHz were observed in the ENDOR spectra from P700+ globally labeled with 15N and specifically labeled with [15N]histidine. These peaks disappeared in "reverse" labeled samples in which all nitrogens are 15N except those of histidine, which contains natural abundance 14N. The dipolar contribution to the hyperfine coupling was determined by using electron spin echo envelope modulation spectroscopy (ESEEM). Numerical simulations of the ESEEM data suggest that the coupling is primarily isotropic and that the histidine is directly coordinated to the central Mg2+ of P700+. Taken together, these data are supportive of a model of P700+ in which the excited state molecular orbital makes a significant contribution to the electronic structure of the radical. Moreover, the methodology developed in this work can be extended to examine the magnetic properties of axial ligands in a variety of biologically relevant porphyrin/chlorin systems.
Assuntos
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Base de dados: MEDLINE Assunto principal: Complexo de Proteínas do Centro de Reação Fotossintética / Histidina Tipo de estudo: Diagnostic_studies Idioma: En Revista: Biochemistry Ano de publicação: 1996 Tipo de documento: Article País de afiliação: Estados Unidos
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Base de dados: MEDLINE Assunto principal: Complexo de Proteínas do Centro de Reação Fotossintética / Histidina Tipo de estudo: Diagnostic_studies Idioma: En Revista: Biochemistry Ano de publicação: 1996 Tipo de documento: Article País de afiliação: Estados Unidos