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.

Usage, Ligands, Ligands (Chemistry), Raman spectroscopy, Solvents

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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.

Nitric oxide, Chemical reactions, Hemoproteins

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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.

Ligand binding (Biochemistry)

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