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Home / Equine Research Bank / J Am Chem Soc / The distal pocket histidine residue in horse heart myoglobin...
Journal of the American Chemical Society2009; 131(50); 18119-18128; doi: 10.1021/ja904726q

The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.

Abstract: It is now well-established that mammalian heme proteins are reactive with various nitrogen oxide species and that these reactions may play significant roles in mammalian physiology. For example, the ferrous heme protein myoglobin (Mb) has been shown to reduce nitrite (NO(2)(-)) to nitric oxide (NO) under hypoxic conditions. We demonstrate here that the distal pocket histidine residue (His64) of horse heart metMb(III) (i.e., ferric Mb(III)) has marked effects on the mode of nitrite ion coordination to the iron center. X-ray crystal structures were determined for the mutant proteins metMb(III) H64V (2.0 A resolution) and its nitrite ion adduct metMb(III) H64V-nitrite (1.95 A resolution), and metMb(III) H64V/V67R (1.9 A resolution) and its nitrite ion adduct metMb(III) H64V/V67R-nitrite (2.0 A resolution). These are compared to the known structures of wild-type (wt) hh metMb(III) and its nitrite ion adduct hh metMb(III)-nitrite, which binds NO(2)(-) via an O-atom in a trans-FeONO configuration. Unlike wt metMb(III), no axial H(2)O is evident in either of the metMb(III) mutant structures. In the ferric H64V-nitrite structure, replacement of the distal His residue with Val alters the binding mode of nitrite from the nitrito (O-binding) form in the wild-type protein to a weakly bound nitro (N-binding) form. Reintroducing a H-bonding residue in the H64V/V67R double mutant restores the O-binding mode of nitrite. We have also examined the effects of these mutations on reactivities of the metMb(III)s with cysteine as a reducing agent and of the (ferrous) Mb(II)s with nitrite ion under anaerobic conditions. The Mb(II)s were generated by reduction of the Mb(III) precursors in a second-order reaction with cysteine, the rate constants for this step following the order H64V/V67R > H64V >> wt. The rate constants for the oxidation of the Mb(II)s by nitrite (giving NO as the other product) follow the order wt > H64V/V67R >> H64V and suggest a significant role of the distal pocket H-bonding residue in nitrite reduction.
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Publication Date: 2009-11-21 PubMed ID: 19924902PubMed Central: PMC2824769DOI: 10.1021/ja904726qGoogle Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research focuses on understanding how the distal pocket histidine residue in horse heart myoglobin affects the mechanism of nitrite ion coordination to the iron center. This interaction is important for numerous biological physiological roles. The research incorporated a comparative analytic approach, using mutant proteins and x-ray crystal structures to compare the effects brought about by mutations in the myoglobin structure.

Objectives

  • The main aim of this research was to explore what influence the distal pocket histidine residue (His64) of horse heart metMb(III), a type of heme protein or ferric Mb(III), has on how nitrite ion links to the iron center.
  • It aimed to understand the changes in coordination of nitrite ions derived from the replacing the distal His residue and how it impacts the reducing effect of cysteine on myoglobin.

Methods

  • The researchers used mutant versions of the proteins metMb(III) H64V and metMb(III) H64V/V67R and their nitrite ion adduct versions for this study.
  • They determined the X-ray crystal structures of these mutant proteins and compared them to the known structures of wild-type hh metMb(III) and its nitrite ion adduct.

Findings

  • The analysis revealed that replacing the distal His (Histidine) residue with Val (Valine) altered the binding mode of nitrite from the nitrito (O-binding) form in the wild-type protein to a weakly bound nitro (N-binding) form.
  • Upon reintroducing a H-bonding residue in the H64V/V67R double mutant, they noticed that the O-binding mode of nitrite was restored.
  • Examination of how these mutations affected the reactivities of the metMb(III)s with cysteine (a reducing agent) and of the ferrous Mb(II)s with nitrite ion under anaerobic conditions revealed the distal pocket H-bonding residue plays a significant role in nitrite reduction.

Conclusion

  • The research suggests a compelling role of the distal pocket H-bonding residue in the reduction of nitrite. The structure of mutant proteins and the subsequent changes in bonding and reduction patterns provide insights into the biochemistry of heme proteins and their interaction with nitrogen oxide species.

Cite This Article

APA
Yi J, Heinecke J, Tan H, Ford PC, Richter-Addo GB. (2009). The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron. J Am Chem Soc, 131(50), 18119-18128. https://doi.org/10.1021/ja904726q

Publication

Journal of the American Chemical Society
ISSN: 1520-5126
NlmUniqueID: 7503056
Country: United States
Language: English
Volume: 131
Issue: 50
Pages: 18119-18128

Researcher Affiliations

Yi, Jun
  • Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, Oklahoma 73019, USA.
Heinecke, Julie
    Tan, Hui
      Ford, Peter C
        Richter-Addo, George B

          MeSH Terms

          • Animals
          • Crystallography, X-Ray
          • Heme / chemistry
          • Histidine / chemistry
          • Histidine / genetics
          • Horses
          • Hydrogen Bonding
          • Iron / chemistry
          • Metmyoglobin / chemistry
          • Metmyoglobin / genetics
          • Models, Molecular
          • Mutagenesis, Site-Directed
          • Mutation
          • Myocardium / chemistry
          • Nitrites / chemistry
          • Oxidation-Reduction
          • Plasmids
          • Protein Binding
          • Protein Conformation
          • X-Ray Diffraction

          Grant Funding

          • R56 GM064476 / NIGMS NIH HHS
          • R56 GM064476-05 / NIGMS NIH HHS
          • GM076640 / NIGMS NIH HHS

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