Nitric oxide heme interactions in nitrophorin from Cimex lectularius

被引:0
作者
R. Christmann
H. Auerbach
R. E. Berry
F. A. Walker
V. Schünemann
机构
[1] University of Kaiserslautern,Department of Physics
[2] The University of Arizona,Department of Chemistry and Biochemistry
来源
Hyperfine Interactions | 2016年 / 237卷
关键词
Nitric oxide; Mössbauer spectroscopy; Density functional theory; Nitrophorin; Heme;
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摘要
The nitrophorin from the bedbug Cimex lectularius (cNP) is a nitric oxide (NO) carrying protein. Like the nitrophorins (rNPs) from the kissing bug Rhodnius prolixus, cNP forms a stable heme Fe(III)-NO complex, where the NO can be stored reversibly for a long period of time. In both cases, the NPs are found in the salivary glands of blood-sucking bugs. The insects use the nitrophorins to transport the NO to the victim’s tissues, resulting in vasodilation and reduced blood coagulation. However, the structure of cNP is significantly different to those of the rNPs from Rhodnius prolixus. Furthermore, the cNP can bind a second NO molecule to the proximal heme cysteine when present at higher concentrations. High field Mössbauer spectroscopy on 57Fe enriched cNP complexed with NO shows reduction of the heme iron and formation of a ferrous nitric oxide (Fe(II)-NO) complex. Density functional theory calculations reproduce the experimental Mössbauer parameters and confirm this observation.
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