Time-resolved UV resonance Raman detection of a transient open form of the ligand pathway in Tyr64(E7) myoglobin
Article Abstract:
A study was conducted to analyze a transient open form of the ligand pathway in Tyr64(E7) myoglobin. Time-resolved ultraviolet resonance Raman experiments were performed to examine the mechanism of ligand entry. A probe beam was generated by the H2-first Stokes shift of the third harmonic of an Nd:YAG laser. Experimental results indicated the presence of the transient conformation wherein Tyr64 swings out of the heme pocket and is subjected to solvent.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
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Resonance Raman investigation of Fe-N-O structure of nitrosylheme in myoglobin and its mutants
Article Abstract:
Interactions of nitric oxide with a heme in proteins have become a particularly interesting area of research. A study therefore investigated the resonance Raman spectra of nitric oxide adducts of mutated myoglobin proteins with particular attention to the Fe-histidine stretching and N-O stretching mode frequency bands to elucidate the resonance Raman spectra of the NO adduct. Experimental materials, methods, results and conclusions are discussed.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1999
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Bound CO is a molecular probe of electrostatic potential in the distal pocket of myoglobin
Article Abstract:
The peaks of the infrared spectrum of carbon monoxide bound to myoglobin can be seen as a sensitive measure of electrostatic fields near the ligand binding site. Electrostatic analyses of ligand binding and Vc-o seem to be applicable in general to heme proteins.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1999
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