Determination of the Fe-CO bond energy in myoglobin using heterodyne-detected transient thermal phase granting spectroscopy

Article Abstract:

The photolysis and rebinding kinetics of carboxy-myoglobin (MbCO) embedded in a trehalose glass at room temperature using transient absorption and diffractive optics-based phase grating spectroscopy on nanosecond to microsecond time scale was investigated. The result suggests that protein structure plays a significant role in the bond energies at active sites which in turn provides a tuning element of the effective barrier heights independent to the transition state region.

Binding energy

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Intermolecular interaction of myoglobin with water molecules along the pH denaturation curve

Article Abstract:

A method for diffusion coefficient (D) measurement for proteins based on the pulsed laser-induced transient grating method using a photosensitive cross-linker is applied to characterize the pH denaturation process of holo- and apo-myoglobin (Mb) from the viewpoint of protein-water interaction. It is found that the pH denaturation curve monitored by D agrees quite well with that determined by the circular dichroism intensity for holo-Mb.

Water, Proteins, Intermolecular forces, Protein denaturation

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Enzyme-like kinetics of ferryloxy myoglobin formation in films on electrodes in microemulsions

Article Abstract:

Covalently linked films of the ferric heme protein myoglobin and poly-L-lysine graphite electrodes reacted with tert-butylhydroperoxide (tBuOOH) to form ferryloxy protein species according to Michaelis-Menten enzyme kinetics. Apparent kinetic constants are most likely governed by acidity-controlled protein conformations and their binding with tBuOOH in the intermediate protein-substrate complex.

Carbon and graphite products, Carbon and Graphite Product Manufacturing, Graphite Contacts & Brushes, Structure, Hemoproteins, Graphite electrodes

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