Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy-Reference-Cited by-同舟云学术

Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy

Published:2017-06-23 Issue:6344 Volume:356 Page:1276-1280
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Mara Michael W.¹²^ORCID,Hadt Ryan G.¹^ORCID,Reinhard Marco Eli³,Kroll Thomas²⁴,Lim Hyeongtaek¹²^ORCID,Hartsock Robert W.³,Alonso-Mori Roberto⁴,Chollet Matthieu⁴,Glownia James M.⁴,Nelson Silke⁴^ORCID,Sokaras Dimosthenis²⁴^ORCID,Kunnus Kristjan³,Hodgson Keith O.¹²^ORCID,Hedman Britt²,Bergmann Uwe³⁴,Gaffney Kelly J.²³^ORCID,Solomon Edward I.¹²^ORCID

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, CA 94305, USA.

2. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.

3. PULSE Institute, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA 94305, USA.

4. Linac Coherent Light Source, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025, USA.

Abstract

Sulfur's balancing act in cytochrome c Cytochrome c enzymes have two distinct functions that depend on the position of a methionine residue. When the sulfur in the methionine side chain coordinates with iron in the enzyme's active site, the protein is optimized for electron transfer; otherwise, it is poised for peroxidase activity. Mara et al. used ultrafast x-ray absorption and emission spectroscopy to probe the energetics of this Fe-S bond (see the Perspective by Bren and Raven). By breaking the bond transiently with light and then timing its reformation, they determined that the surrounding protein environment boosts the bond strength by 4 kilocalories per mole—just enough to toggle between each functional state at a practical rate. Science , this issue p. 1276 ; see also p. 1236

Funder

National Institutes of Health

U.S. Department of Energy

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference46 articles.

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2. G. W. Pettigrew G. R. Moore Cytochromes c: Biological Aspects (Springer-Verlag 1987).

3. Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers

4. Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function

5. Copper coordination in blue proteins

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