Active site structure in cytochrome c peroxidase and myoglobin mutants: effects of altered hydrogen bonding to the proximal histidine

Biochemistry
R SinclairL Powers

Abstract

The globins and peroxidases, while performing completely different chemistry, share features of the iron heme active site: a protoporphyrin IX prosthetic group is linked to the protein by the proximal histidine residue. X-ray absorption spectroscopy provides a method to determine the local structure of iron heme active sites in proteins. Our previous studies using X-ray absorption spectroscopy revealed a significant difference in the Fe-N epsilon bond length between the peroxidases and the globins [for a review, see Powers, L. (1994) Molecular Electronics and Molecular Electronic Devices, Vol. 3, p 211 CRC Press Inc., Boca Raton, FL]. Globins typically have an Fe-N epsilon distance close to 2.1 A while the Fe-N epsilon distance in the peroxidases is closer to 1.9 A. We have proposed [Sinclair, R., Powers, L., Bumpus, J., Albo, A., & Brock, B. (1992) Biochemistry 31, 4892] that strong hydrogen bonding to the proximal histidine is responsible for the shorter bond length in the peroxidases. Here we use site-specific mutagenesis to eliminate the strong proximal hydrogen bonding in cytochrome c peroxidase and to introduce strong proximal hydrogen bonding in myoglobin. Consistent with our hypothesis, elimination of the Asp235-His175 ...Continue Reading

Citations

Nov 3, 2001·Biochimica Et Biophysica Acta·A BonamoreA Boffi
Sep 29, 2011·Biochemistry·Edward L D'AntonioStefan Franzen
Mar 3, 2009·The Journal of Biological Chemistry·Virve RauhamäkiMårten Wikström
Mar 27, 2002·Archives of Biochemistry and Biophysics·Deborah K JonesEmma Lloyd Raven
Feb 26, 2016·International Journal of Biological Macromolecules·Kazem AsadollahiMojtaba Falahati
Aug 1, 2000·Environmental Science & Technology·J A Macdonald
May 23, 2018·Chemistry : a European Journal·Takahiro HayashiAnthony P Green
Jul 2, 2019·Journal of the Science of Food and Agriculture·Sara RagucciAntimo Di Maro

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