Resonance Raman spectroscopy shows different temperature-dependent coordination equilibria for native horseradish and cytochrome c peroxidase
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چکیده
منابع مشابه
Resonance Raman spectroscopy of horseradish peroxidase derivatives and intermediates with excitation in the near ultraviolet.
Resonance Raman enhancement of derivatives and intermediates of horseradish peroxidase in the near ultraviolet (N-band excitation) results in intensity and enhancement patterns that are different from those normally observed within the porphyrin Soret (B-band) and alpha-beta (Q-band) absorptions. In particular it allows the resolution of resonance Raman spectra of horseradish peroxidase compoun...
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Temperature-dependent photodegradation during UV-resonance Raman spectroscopy was investigated. Photodegradation was quantitatively probed by monitoring the temporal evolution of UV-resonance Raman spectra obtained from bacteriochlorophyll (BChl) showing, resonance effect at a 355-nm excitation wavelength. At 80 K, the molecular photodecomposition rate was 5-times lower than that at room temper...
متن کاملHigh-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase.
Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H(2)O(2) to 2H(2)O by oxidizing two molecules of cytochrome c (cyt c). Here we compare the 1.2 A native structure (CCP) with the 1.3 A structure of its stable oxidized reaction intermediate, Compound I (CCP1). In addition, crystals were analyzed by UV-vis abso...
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Acriflavine (3,6-diaminoacridine) is an anticeptic drug developed in 1912. Previous research has focused on investigation of the intercalating features of acriflavine, but little is known about its interaction with proteins. Drug-receptor interaction is of major interest in clinical science. The aim of the present study was to evaluate the ability of acriflavine to induce alterations in conform...
متن کاملElectron transfer and electrocatalytics of cytochrome c and horseradish peroxidase on DNA modified electrode.
A bio-interphase composed of DNA, cytochrome c (Cyt c) and horseradish peroxidase (HRP) was developed by layer-by-layer assembling Cyt c, DNA and Cyt c-HRP on biocompatible 11-mercaptoundecanoic acid--6-mercapto-1-hexanol modified gold electrode. The new bio-interphase was used as a model system to mimic the electron transfer and electrocatalytic performance of two proteins in living organisms....
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1985
ISSN: 0014-5793
DOI: 10.1016/0014-5793(85)81288-6