| review article | Q7318358 |
| scholarly article | Q13442814 |
| P356 | DOI | 10.1002/(SICI)1520-6343(1999)5:5+<S3::AID-BSPY2>3.0.CO;2-P |
| P698 | PubMed publication ID | 10512534 |
| P2093 | author name string | Roger G | |
| Bertrand P | |||
| Belle V | |||
| Fournel A | |||
| Guigliarelli B | |||
| More C | |||
| Asso M | |||
| P2860 | cites work | Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S] | Q27641437 |
| Refined structure of cytochrome c3 at 1.8 A resolution | Q27729136 | ||
| Crystal structure of cytochrome c3 from Desulfovibrio desulfuricans Norway at 1.7 A resolution | Q27730760 | ||
| Solution structure of Desulfovibrio vulgaris (Hildenborough) ferrocytochrome c3: structural basis for functional cooperativity | Q27765154 | ||
| A method for distance determination in proteins using a designed metal ion binding site and site-directed spin labeling: evaluation with T4 lysozyme | Q33666023 | ||
| EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism | Q33968909 | ||
| EPR determination of the oxidation-reduction potentials of the hemes in cytochrome c3 from Desulfovibrio vulgaris | Q40157801 | ||
| Individual redox characteristics and kinetic properties of the hemes in cytochromes c3: new methods of investigation | Q40606803 | ||
| The chemistry of xanthine oxidase. Electron-spin resonance of xanthine oxidase solutions | Q41915416 | ||
| Cytochrome c3 from Desulfovibrio gigas: crystal structure at 1.8 A resolution and evidence for a specific calcium-binding site | Q42845388 | ||
| Copper(II)-substituted horse liver alcohol dehydrogenase: structure of the minor species | Q45212748 | ||
| Modified ligands to FA and FB in photosystem I. I. Structural constraints for the formation of iron-sulfur clusters in free and rebound PsaC. | Q46662376 | ||
| Further characterization of the two tetraheme cytochromes c3 from Desulfovibiro africanus: nucleotide sequences, EPR spectroscopy and biological activity | Q48042060 | ||
| Regulation of the redox order of four hemes by pH in cytochrome c3 from D. vulgaris Miyazaki F. | Q48786615 | ||
| EPR study of the redox interactions in cytochrome c3 from Desulfovibrio vulgaris Miyazaki. | Q52531893 | ||
| EPR determination of interaction redox potentials in a multiheme cytochrome: cytochrome c3 from Desulfovibrio desulfuricans Norway. | Q52551202 | ||
| Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes. | Q54657276 | ||
| Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer. | Q54726616 | ||
| The Mononuclear Molybdenum Enzymes. | Q55035690 | ||
| Temperature-Jump and Potentiometric Studies on Recombinant Wild Type and Y143F and Y254F Mutants ofSaccharomyces cerevisiaeFlavocytochromeb2: Role of the Driving Force in Intramolecular Electron Transfer Kinetics†,‡ | Q58070525 | ||
| Single-crystal electron paramagnetic resonance study of cytochrome c3 from Desulfovibrio desulfuricans Norway Strain. Assignment of the heme midpoint redox potentials | Q68484344 | ||
| Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters | Q71145562 | ||
| Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes | Q72956165 | ||
| Nature and electronic structure of the Ni-X dinuclear center of Desulfovibrio gigas hydrogenase. Implications for the enzymatic mechanism | Q73456128 | ||
| Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A | Q73770448 | ||
| Orbital Configuration of the Valence Electrons, Ligand Field Symmetry, and Manganese Oxidation States of the Photosynthetic Water Oxidizing Complex: Analysis of the S(2) State Multiline EPR Signals | Q74821072 | ||
| P433 | issue | 5 Suppl | |
| P304 | page(s) | S3-18 | |
| P577 | publication date | 1999-01-01 | |
| P1433 | published in | Biospectroscopy | Q27714316 |
| P1476 | title | EPR spectroscopy: a powerful technique for the structural and functional investigation of metalloproteins | |
| P478 | volume | 5 |
| Q34977961 | Cardiolipin-based respiratory complex activation in bacteria. |
| Q34166732 | Characterization of Cupriavidus metallidurans CYP116B1--a thiocarbamate herbicide oxygenating P450-phthalate dioxygenase reductase fusion protein |
| Q37395595 | Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes |
| Q48181699 | Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels |
| Q33976954 | Q-cycle bypass reactions at the Qo site of the cytochrome bc1 (and related) complexes |
| Q34391356 | The Methylococcus capsulatus (Bath) secreted protein, MopE*, binds both reduced and oxidized copper |
| Q57985916 | The Structure of Acidithiobacillus ferrooxidans c4-Cytochrome |
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