Solvent isotope effects on NMR spectral parameters in high-spin ferric hemoproteins: an indirect probe for distal hydrogen bonding.

La Mar, G N; Chatfield, M J; Peyton, D H; de Ropp, J S; Smith, W S; Krishnamoorthi, R; Satterlee, J D; Erman, J E

La Mar, G N; Chatfield, M J; Peyton, D H; de Ropp, J S; Smith, W S; Krishnamoorthi, R; Satterlee, J D; Erman, J E.

Affiliation

La Mar GN; Department of Chemistry, University of California, Davis 95616.

Biochim Biophys Acta ; 956(3): 267-76, 1988 Oct 12.

Article in En | MEDLINE | ID: mdl-2844271

Subject(s)

Hemeproteins/metabolism; Animals; Cytochrome c Group/metabolism; Cytochrome-c Peroxidase/metabolism; Hemoglobins/metabolism; Horseradish Peroxidase/metabolism; Humans; Hydrogen; Hydrogen Bonding; Magnetic Resonance Spectroscopy/methods; Metmyoglobin/metabolism; Myoglobin/analogs & derivatives; Myoglobin/metabolism; Protein Conformation

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Collection: 01-internacional Database: MEDLINE Main subject: Hemeproteins Limits: Animals / Humans Language: En Journal: Biochim Biophys Acta Year: 1988 Type: Article

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PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Hemeproteins Limits: Animals / Humans Language: En Journal: Biochim Biophys Acta Year: 1988 Type: Article