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Describes the interaction of the hepatitis C virus (HCV) NS3 protease domain with its NS4A cofactor peptide at equilibrium and at pre-steady state under different physiochemical conditions. Extent of glycerol-induced stabilization varied in an HCV strain-dependent way with at least one determinant mapping to an NS3 interaction site.

Examines the complex formation between the hepatitis C virus serine protease and A synthetic NS4A cofactor peptide. Maturation cleavages that occur in the nonstructural region of the viral protein; In vitro complex formation between the NS3 protease domain.

Presents a homology model that predicts the components of the zinc binding site of the serine protease domain of NS3 protein of hepatitis C virus. Need of zinc for enzymatic activity; Properties of the metal-substituted NS3 proteinases.

Examines the ferrous five-coordinate nitrosylheme b[sub 3] complex in cytochrome cbb[sub 3] oxidase from Pseudomonas stutzeri by resonance raman spectrometry. Chemistry of nitric oxide interactions; Inhibition of cytochrome oxidase by nitrite; Phylogeny of aerobic respiration and bacterial denitrification.

States that the nonstructural protein NS3 of the hepatitis C virus (HCV), harbors a serine protease domain that is responsible for most of the processing events of the nonstructural region of the polyprotein. How inhibition of NS3 affects the disease caused by HCV; Methodology used to conduct inhibition process; Identification of an important determinant for product binding; Discussion on findings.

Examines the influence of the heme Fe-CO complex of cytochrome cbb[sub 3]-CO at ambient temperature formation on the decay of the transient Cu[sub B]-CO complex. Use of time-resolved fourier transform infrared spectroscopy; Catalyzation of molecular oxygen reduction by the complex; Importance of photodynamics of cbb[sub 3]-CO for elucidating the mechanisms for legal entry/exit in heme-cooper oxidase.