Effects of distal pocket mutations on the geminate recombination of NO with leghemoglobin on the picosecond time scale

Article Abstract:

The picosecond NO geminate kinetics rebinding of a monomeric plant hemoglobin with structural similarity to myoglobin, wild-type hemoglobin, and the six mutant proteins at the distal histidine are investigated. Certain proximal mutations may possibly influence the distal barrier or the distal barrier is influenced by the impact of the dissociated ligand.

Hemoglobin, Hemoglobins, Ligand binding (Biochemistry), Chemical properties

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Effects of distal pocket mutations on the geminate recombination of NO with leghemoglobin on the picosecond time scale

Article Abstract:

The picosecond NO geminate kinetics rebinding of a monomeric plant hemoglobin with structural similarity to myoglobin, wild-type hemoglobin, and the six mutant proteins at the distal histidine are investigated. Certain proximal mutations may possibly influence the distal barrier or the distal barrier is influenced by the impact of the dissociated ligand.

Observations, Proteins, Chemical reaction, Rate of, Chemical kinetics

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A comparative femtosecond coherence study of the unligated monomeric hemeproteins myoglobin and leghemoglobin

Article Abstract:

Vibrational coherences in leghemoglobin are reported and a comparative study with the widely studied system, myoglobin is discussed. Impulsive optical excitation was performed on leghemoglobin and it showed a decrease in vibrational amplitude as compared to myoglobin.

Analysis, Myoglobin, Optical properties, Vibrational spectra

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