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Solid-State NMR Reveals Structural and Dynamical Properties of a Membrane-Anchored Electron-Carrier Protein, Cytochrome b₅

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Ulrich H. N. Dürr,^† Kazutoshi Yamamoto,^† Sang-Choul Im,^‡ Lucy Waskell,^‡ and Ayyalusamy Ramamoorthy*^†

Biophysics Research Division and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, and Department of Anesthesiology, University of Michigan, and VA Medical Center, Ann Arbor, Michigan 48105

J. Am. Chem. Soc., 2007, 129 (21), pp 6670–6671

DOI: 10.1021/ja069028m

Publication Date (Web): May 9, 2007

†

Biophysics Research Division and Department of Chemistry.

‡

Department of Anesthesiology and VA Medical Center.

In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

, ramamoor@umich.edu

Abstract

Cytochrome b₅ (cyt b₅) is a membrane-anchored electron-carrier protein containing a heme in its soluble domain. It enhances the enzymatic turnover of selected members of the cytochrome P450 superfamily of catabolic enzymes, localized in the endoplasmic reticulum of liver cells. Remarkably, its α-helical membrane-anchoring domain is indispensable for the cyt b₅/cyt P450 interaction. Here, we present the first solid-state NMR studies on holo-cyt b₅ in a membrane environment, namely, macroscopically oriented DMPC:DHPC bicelles. We have presented approaches to selectively investigate different domains of the protein using spectral editing NMR techniques that utilize the unique motional properties of each domain. Two-dimensional ¹H−¹⁵N HIMSELF spectra showed PISA-wheel patterns reporting on the structure and dynamics of the membrane anchor of the protein.

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Published In Issue May 30, 2007
Received December 17, 2006

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Communication

Solid-State NMR Reveals Structural and Dynamical Properties of a Membrane-Anchored Electron-Carrier Protein, Cytochrome b₅