Conformational Mobility in the Active Site of a Heme Peroxidase
Open Access
- 1 August 2006
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 281 (34) , 24512-24520
- https://doi.org/10.1074/jbc.m602602200
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Autocatalytic Formation of Green Heme: Evidence for H2O2-Dependent Formation of a Covalent Methionine−Heme Linkage in Ascorbate PeroxidaseJournal of the American Chemical Society, 2004
- Substrate Binding and Catalytic Mechanism in Ascorbate Peroxidase: Evidence for Two Ascorbate Binding SitesBiochemistry, 2002
- Formation of a Bis(histidyl) Heme Iron Complex in Manganese Peroxidase at High pH and Restoration of the Native Enzyme Structure by CalciumBiochemistry, 2000
- A study of the K+-site mutant of ascorbate peroxidase: mutations of protein residues on the proximal side of the heme cause changes in iron ligation on the distal sideJBIC Journal of Biological Inorganic Chemistry, 1999
- Class I Heme Peroxidases: Characterization of Soybean Ascorbate PeroxidaseArchives of Biochemistry and Biophysics, 1998
- Role of Calcium in Maintaining the Heme Environment of Manganese PeroxidaseBiochemistry, 1997
- pH, Electrolyte, and Substrate-Linked Variation in Active Site Structure of the Trp51Ala Variant of Cytochrome c PeroxidaseBiochemistry, 1995
- Effect of Asp-235 .fwdarw. Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidaseBiochemistry, 1992
- Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidaseBiochemistry, 1991
- Enthalpy of decomposition of hydrogen peroxide by catalase at 25° C (with molar extinction coefficients of H2O2 solutions in the UV)Analytical Biochemistry, 1972