期刊
BIOCHEMISTRY
卷 55, 期 41, 页码 5809-5817出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00775
关键词
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资金
- Iowa State University College of Liberal Arts and Sciences Signature Research Initiative
Reduction of hydroxylamine to ammonium by-phytoglobin, a plant hexacoordinate hemoglobin, is much faster than that of other hexacoordinate hemoglobins. or pentacoordinate hemoglobins, such as myoglobin, leghemoglobin, and red blood cell hemoglobin. The reason-for differences in reactivity is not known, but could be intermolecular electron transfer between protein molecules in support of the required two-electron reduction) hydroxylamine binding, or active site architecture favoring the reaction. Experiments were conducted with phytoglobins from rice, tomato, and soybean along with human neuroglobin and soybean leghemoglobin that reveal hydroxylamine binding- as the rate-limiting step. For hexacoordinate hemoglobins, binding is limited by the dissociation rate constant for the distal histidine, while leghemoglobin is limited by an intrinsically low affinity for hydroxylamine. When the distal histidine is removed from rice phytoglobin, a hydroxylamine-bound intermediate is formed and the reaction rate is diminished, indicating that the distal histidine imidazole side chain is critical for the reaction, albeit not for electron transfer but rather for direct interaction with the substrate. Together, these results demonstrate that phytoglobins are superior at hydroxylamine reduction because they have distal-histidine: coordination affinity constants near 1, and facile rate constants for binding and dissociation of the histidine aide Chain. Hexacoordinate hemoglobins such as neuroglobin are limited by tighter histidine coordination that blocks hydroxylamine binding, and pentacoordinate hemoglobins have intrinsically lower hydroxylamine affinities.
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