Camfree us nm
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A similar conformational switching mechanism is thought to enable electron transfer through the FMN domain in the related flavoproteins NADPH-cytochrome P450 reductase and methionine synthase reductase (38) The n NOSr ribbon structure (from PDB: 1TLL) showing bound FAD (yellow) in FNR domain (green), FMN (orange) in FMN domain (yellow), connecting hinge (blue), and the Cy3–Cy5 label positions (pink) and distance (42 Å, dashed line).
Transitions between these states can occur on a variety of length scales (Å to nm) and time scales (ps to s) and have been linked to functionally relevant phenomena such as allosteric signaling, enzyme catalysis, and protein–protein interactions (2–11).
It is difficult to characterize such spatially and temporally inhomogeneous dynamics in bulk solution by an ensemble-averaged measurement, especially in proteins that undergo multiple-conformation transformations.
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The ability of Ca M, or similar signaling proteins, to regulate electron transfer reactions in enzymes is unusual, and the mechanism is a topic of interest and intensive study.
It has long been known that Ca M binding alters NOSr structure such that, on average, it populates a more open conformation (43, 44).
( reductase activity of n NOSr proteins in their Ca M-bound and Ca M-free states.
Color scheme of bar graphs: Black, WT n NOSr unlabeled; Red, Cys-lite (CL) n NOSr unlabeled; Blue, E827C/Q1268C CL n NOSr unlabeled; and Dark cyan, E827C/Q1268C CL n NOSr labeled.) The n NOSr ribbon structure (from PDB: 1TLL) showing bound FAD (yellow) in FNR domain (green), FMN (orange) in FMN domain (yellow), connecting hinge (blue), and the Cy3–Cy5 label positions (pink) and distance (42 Å, dashed line).
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