- Reduction Potentials of Rieske Clusters: Importance of the Coupling between Oxidation State and Histidine Protonation State
- Identification of Hydrogen Bonds to the Rieske Cluster through the Weakly Coupled Nitrogens Detected by Electron Spin
- Mechanism of Ubiquinol Oxidation by the bc1 Complex: Role of the Iron Sulfur Protein and Its Mobility
- Exploration of Ligands to the Qi Site Semiquinone in the bc1 Complex Using High-resolution EPR*
- Life, Information, Entropy, Vehicles for Semantic Inheritance
- Nature Macmillan Publishers Ltd 1998 NATURE |VOL 392 |16 APRIL 1998 677
- Steered Molecular Dynamics Simulation of the Rieske Subunit Motion in the Cytochrome bc1 Complex
- T. Wydrzynski and K. Satoh (eds): Photosystem II: The Water/Plastoquinone Oxido-Reductase in Photosynthesis, pp. 000000. 2005 Kluwer Academic Publishers. Printed in The Netherlands.
- Steps toward Constructing a Cytochrome b6 f Complex in the Purple Bacterium Rhodobacter Sphaeroides: An Example of the Structural Plasticity of a Membrane
- Hydrogen Bonds Involved in Binding the Qi-site Semiquinone in the bc1 Complex, Identified through Deuterium Exchange
- Vermglio and Joliot (1) have emphasized their view that the components of the Rhodobacter sphaeroides chain are organized as supercomplexes. This model was
- Modulation of the Midpoint Potential of the [2Fe-2S] Rieske Iron Sulfur Center by Qo Occupants in the bc1 Complex
- Protein-Lipid Interactions in Zein Films Investigated by Surface Plasmon Resonance
- ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY
- Proton-coupled electron transfer at the Qo site: what type of mechanism can account for the high activation barrier?
- Annu. Rev. Physiol. 2004. 66:689733 doi: 10.1146/annurev.physiol.66.032102.150251
- The Energy Landscape for Ubihydroquinone Oxidation at the Qo Site of the bc1 Complex in Rhodobacter sphaeroides*
- Photosynthesis Research 000: 121, 2003. 2003 Kluwer Academic Publishers. Printed in the Netherlands.
- Crofts, A.R., Berry, E.A., Kuras, R., Guergova-Kuras, M., Hong, S. and Ugulava, N. (1998) Structures of the bc1 complex reveal dynamic aspects of mechanism. In "Photo-
- Expression and One-Step Purification of a Fully Active Poly-Histidine Tagged Cytochrome bc1-Complex from Rhodobacter sphaeroides.
- Physicochemical Aspects of the Movement of the Rieske Iron Sulfur Protein during Quinol Oxidation by the bc1 Complex from Mitochondria and Photosynthetic
- Specific Mutagenesis of the Rieske Iron-Sulfur Protein in Rhodobacter sphaeroides Shows That both the Thermodynamic Gradient and the pK of the Oxidized Form
- Aspartate-187 of Cytochrome b Is Not Needed for DCCD Inhibition of Ubiquinol: Cytochrome c Oxidoreductase in Rhodobacter sphaeroides Chromatophores
- DCCD Inhibits the Reactions of the Iron-Sulfur Protein in Rhodobacter sphaeroides Chromatophores
- The Electric Field Generated by Photosynthetic Reaction Center Induces Rapid Reversed Electron Transfer in the bc1 Complex
- The Interaction of the Rieske Iron-Sulfur Protein with
- Interactions of quinone with the ironsulfur protein of the bc1 complex: is the mechanism spring-loaded?
- The Modified Q-cycle Explains the Apparent Mismatch between the Kinetics of Reduction of Cytochromes c1 and bH in the bc1 Complex*
- Proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
- Spectral analysis of the bc1 complex components in situ: Beyond the traditional difference approach
- RESEARCH PAPER The differential effects of herbivory by first and fourth
- In Situ Kinetics of Cytochromes c1 and c2 Vladimir P. Shinkarev,* Antony R. Crofts, and Colin A. Wraight
- Hydrogen Bonds between Nitrogen Donors and the Semiquinone in the Qi-site of the bc1 Complex*
- Rapid report Marcus treatment of endergonic reactions: A commentary
- Vermglio has brought up a number of interesting points. 1) Statistical models. It would be helpful if the authors could agree that either statistical model
- Disentangling entanglement Antony R. Crofts
- Progress has recently been made in the understanding of the function of the cytochrome bc1 complex and related
- Mechanism of Ubiquinol Oxidation by the bc1 Complex: Role of the Iron Sulfur Protein and Its Mobility
- Photosystem II Peripheral Accessory Chlorophyll Mutants in Chlamydomonas reinhardtii. Biochemical
- Proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation.
- The bc1 Complex: What is There Left to Argue About?
- Impact of folivory on photosynthesis is greater than the sum of its holes
- Proton processing at the Qo-site of the bc1 complex of Rhodobacter sphaeroides
- Atomic Resolution Structures of Rieske Iron-Sulfur Protein: Role of Hydrogen Bonds in Tuning
- Multiple Q-Cycle Bypass Reactions at the Qo Site of the Cytochrome bc1 Complex Florian Muller, Antony R. Crofts, and David M. Kramer*,
- CD-monitored redox titration of the Rieske Fe-S protein of Rhodobacter sphaeroides: pH dependence of the midpoint potential
- Proton pumping in the bc1 complex: A new gating mechanism that prevents short circuits
- Mechanism of Ubiquinol Oxidation by the bc1 Complex: Different Domains of the Quinol Binding Pocket and Their Role in the Mechanism and Binding of Inhibitors
- Mechanistic aspects of the Qo-site of the bc1-complex as re-vealed by mutagenesis studies, and the crystallographic
- Spectral and kinetic resolution of the bc1 complex components in situ: A simple and robust alternative to the traditional difference
- Annu. Rev. Biochem. 2000. 69:100575 Copyright c 2000 by Annual Reviews. All rights reserved
- 10.1110/ps.052035406Access the most recent version at doi: 2006 15: 2019-2024Protein Sci.
- Photosynthesis Research 55: 357362, 1998. 1998 Kluwer Academic Publishers. Printed in the Netherlands.
- Characterization of the pH-Dependent Resonance Raman Transitions of Archaeal and Bacterial Rieske [2Fe-2S] Proteins
