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Innovations in X-ray Absorption and Optical Spectroscopy: Insights from Myoglobin and Cytochrome Peroxidases

This document explores groundbreaking research in X-ray absorption and optical spectroscopy, focusing on the structural and functional similarities between various peroxidases and myoglobin. Significant findings include the impact of proximal histidine on hydrogen bonding, influencing iron-heme interactions and ligand distances. Key contributions from researchers such as Britton Chance and his collaborators are highlighted, shedding light on peroxidase intermediates, geminate states, and the intricate dynamics of these essential biological catalysts.

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Innovations in X-ray Absorption and Optical Spectroscopy: Insights from Myoglobin and Cytochrome Peroxidases

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  1. A Beacon for Creativity and Innovation Britton Chance

  2. Instrumentation for X-ray Absorption and Optical Spectroscopy

  3. Active Site Similarity of Myoglobin Peroxidase with Peroxidase Intermediates Chance, Powers, Ching, Poulos, Yamazaki 1984 M Chance, Powers, Kumar, Chance 1986 M Chance, Powers, Poulos, Chance 1986

  4. Effects of Proximal Histidine Altered H-bonding CcP D235N CcP W191F Mb L89D Mb L89V Mb L89I cytochrome c peroxidase [CcP] myoglobin [Mb] H-bonding to proximal histidine controls Fe- heme nitrogen distances O ligand distance Sinclair, Hallam, Chen, Chance, Powers 1996

  5. Peroxidatic Form of Cytochrome c Oxidase Kumar, Naqui, Powers, Ching, Chance 1988

  6. Geminate States of MbCO Chance, Fischetti, Powers 1983 Powers, Sessler, Woolery, Chance 1984 Powers, Chance, M Chance, Campbell, Friedman, et al 1987

  7. Stories Egret Marathon Teotihuacan

  8. Thank You, BC!

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