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| {{STRUCTURE_1f5b| PDB=1f5b | SCENE= }} | | {{STRUCTURE_1f5b| PDB=1f5b | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF F2H FERREDOXIN 1 MUTANT FROM AZOTOBACTER VINELANDII AT 1.75 ANGSTROM RESOLUTION'''
| | ===CRYSTAL STRUCTURE OF F2H FERREDOXIN 1 MUTANT FROM AZOTOBACTER VINELANDII AT 1.75 ANGSTROM RESOLUTION=== |
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| ==Overview==
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| Elucidating how proteins control the reduction potentials (E0') of [Fe--S] clusters is a longstanding fundamental problem in bioinorganic chemistry. Two site-directed variants of Azotobacter vinelandii ferredoxin I (FdI) that show large shifts in [Fe--S] cluster E0' (100--200 mV versus standard hydrogen electrode (SHE)) have been characterized. High resolution X-ray structures of F2H and F25H variants in their oxidized forms, and circular dichroism (CD) and electron paramagnetic resonance (EPR) of the reduced forms indicate that the overall structure is not affected by the mutations and reveal that there is no increase in solvent accessibility nor any reorientation of backbone amide dipoles or NH--S bonds. The structures, combined with detailed investigation of the variation of E0' with pH and temperature, show that the largest increases in E0' result from the introduction of positive charge due to protonation of the introduced His residues. The smaller (50--100 mV) increases observed for the neutral form are proposed to occur by directing a Hdelta+--Ndelta- dipole toward the reduced form of the cluster.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11875515}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11875515 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11875515}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Iron sulfur protein]] | | [[Category: Iron sulfur protein]] |
| [[Category: Protein monomer]] | | [[Category: Protein monomer]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:55:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:43:16 2008'' |
