Pages that link to "Q27642325"
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The following pages link to Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 A resolution (Q27642325):
Displaying 28 items.
- Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer (Q24669818) (← links)
- Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin (Q24675963) (← links)
- A metallothionein containing a zinc finger within a four-metal cluster protects a bacterium from zinc toxicity (Q27633997) (← links)
- Structure at 1.0 A resolution of a high-potential iron-sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus (Q27660212) (← links)
- Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity (Q27684501) (← links)
- The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow (Q28492481) (← links)
- Influence of NH-Sgamma bonding interactions on the structure and dynamics of metallothioneins. (Q30378985) (← links)
- Amino acid sequences and distribution of high-potential iron-sulfur proteins that donate electrons to the photosynthetic reaction center in phototropic proteobacteria (Q30882358) (← links)
- Role of aromatic residues in stabilization of the [Fe4S4] cluster in high-potential iron proteins (HiPIPs): physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP. (Q33845598) (← links)
- Structural origins of redox potentials in Fe-S proteins: electrostatic potentials of crystal structures (Q34041198) (← links)
- Fold versus sequence effects on the driving force for protein-mediated electron transfer (Q34082277) (← links)
- Structure-function studies of [2Fe-2S] ferredoxins (Q34329960) (← links)
- Identifying sequence determinants of reduction potentials of metalloproteins (Q34729588) (← links)
- Structural and functional studies on the tetraheme cytochrome subunit and its electron donor proteins: the possible docking mechanisms during the electron transfer reaction (Q36174115) (← links)
- Crystallographic characterization of the high-potential iron-sulfur protein in the oxidized state at 0.8 Å resolution. (Q36381072) (← links)
- Characterizing the effects of the protein environment on the reduction potentials of metalloproteins (Q36596069) (← links)
- Calculating standard reduction potentials of [4Fe-4S] proteins (Q36605137) (← links)
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers (Q37727718) (← links)
- The role of a conserved tyrosine residue in high-potential iron sulfur proteins. (Q41990042) (← links)
- Structural analysis of the HiPIP from the acidophilic bacteria: Acidithiobacillus ferrooxidans (Q43020089) (← links)
- The structure of iron-sulfur proteins (Q43025948) (← links)
- Protein Control of Redox Potentials of Ironminus signSulfur Proteins (Q46276124) (← links)
- Cloning and sequencing of the gene encoding the high potential iron-sulfur protein (HiPIP) from the purple sulfur bacterium Chromatium vinosum (Q48049924) (← links)
- Automatic Solution of Heavy-Atom Substructures (Q56877796) (← links)
- Structure-Property Relationships of Fe4S4Clusters (Q57905327) (← links)
- Reversible Super-Reduction of the Cubane [4Fe-4S](3+;2+;1+) in the High-Potential Iron-Sulfur Protein Under Non-Denaturing Conditions. EPR Spectroscopic and Electrochemical Studies (Q71814267) (← links)
- HiPIP in Rubrivivax gelatinosus is firmly associated to the membrane in a conformation efficient for electron transfer towards the photosynthetic reaction centre (Q73074815) (← links)
- Comparative differential cuproproteomes of Rhodobacter capsulatus reveal novel copper homeostasis related proteins (Q90153840) (← links)