Control of Myoglobin Electron-Transfer Rates by the Distal (Nonbound) Histidine Residue
- 1 January 1996
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (14), 3490-3492
- https://doi.org/10.1021/ja954181u
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- High-Resolution Crystal Structures of Distal Histidine Mutants of Sperm Whale MyoglobinJournal of Molecular Biology, 1993
- Magnetic resonance study of the inclusion compounds of sodium in zeolites: beyond the metal particles modelJournal of the American Chemical Society, 1992
- Site-directed mutagenesis of histidine residues involved in Cu(II) binding and reduction by sperm whale myoglobin.Proceedings of the National Academy of Sciences, 1992
- Direct electron transfer of horse heart myoglobin at an indium oxide electrodeJournal of Electroanalytical Chemistry, 1992
- Effects of Buried Ionizable Amino Acids on the Reduction Potential of Recombinant MyoglobinScience, 1989
- The role of the distal histidine in myoglobin and haemoglobinNature, 1988
- High-level expression of sperm whale myoglobin in Escherichia coli.Proceedings of the National Academy of Sciences, 1987
- Long-distance electron transfer in pentaammineruthenium (histidine-48)-myoglobin. Reorganizational energetics of a high-spin hemeJournal of the American Chemical Society, 1985
- Polarography of Lead(II) in Aqueous Hydrofluoric Acid (1 to 12M) with a Dropping-Mercury Electrode of Teflon.Analytical Chemistry, 1965