CaltechAUTHORS
  A Caltech Library Service

Type-zero copper proteins

Lancaster, Kyle M. and George, Serena DeBeer and Yokoyama, Keiko and Richards, John H. and Gray, Harry B. (2009) Type-zero copper proteins. Nature Chemistry, 1 (9). pp. 711-715. ISSN 1755-4330. PMCID PMC2841405. https://resolver.caltech.edu/CaltechAUTHORS:20100107-092654651

[img] PDF - Accepted Version
See Usage Policy.

2957Kb
[img]
Preview
PDF - Supplemental Material
See Usage Policy.

2637Kb

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20100107-092654651

Abstract

Many proteins contain copper in a range of coordination environments, where it has various biological roles, such as transferring electrons or activating dioxygen. These copper sites can be classified by their function or spectroscopic properties. Those with a single copper atom are either type 1, with an intense absorption band near 600 nm, or type 2, with weak absorption in the visible region. We have built a novel copper(ii) binding site within structurally modified Pseudomonas aeruginosa azurins that does not resemble either existing type, which we therefore call 'type zero'. X-ray crystallographic analysis shows that these sites adopt distorted tetrahedral geometries, with an unusually short Cu–O (G45 carbonyl) bond. Relatively weak absorption near 800 nm and narrow parallel hyperfine splittings in electron paramagnetic resonance spectra are the spectroscopic signatures of type zero copper. Cyclic voltammetric experiments demonstrate that the electron transfer reactivities of type-zero azurins are enhanced relative to that of the corresponding type 2 (C112D) protein.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1038/NCHEM.412 DOIArticle
http://www.nature.com/nchem/journal/v1/n9/abs/nchem.412.htmlPublisherArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2841405/PubMed CentralArticle
Additional Information:© 2009 Macmillan Publishers Limited. Received 5 May 2009; Accepted 15 September 2009; Published online 1 November 2009. We thank B. Brunschwig for assistance with Fourier transform infrared spectroscopy, Z. Gates and L. Thomas for assistance with X-ray diffraction data collection, and M. Day and J. Kaiser for discussions of crystal structural analyses. We thank E. Solomon for helpful comments on electronic structural formulations, and Y. Sheng for assistance with protein expression and purification. Stanford Synchrotron Radiation Lightsource operations are funded by DOE(BES). The Structural Molecular Biology program is supported by NIH (NCRR BMTP) (Grant Number 5 P41 RR001209)N and DOE(BER). This work was supported by NIH DK019038(HBG), Stanford GCEP, and NSF CHE-0802907. The Caltech Molecular Observatory is supported by the Gordon and Betty Moore Foundation. Author Contributions: K.M.L. and H.B.G. conceived and designed the experiments; K.M.L., S.D.G., and K.Y. performed the experiments; K.M.L., S.D.G., K.Y., and H.B.G. analysed the data, K.M.L., S.D.G., J.H.R., and H.B.G. co-wrote the paper.
Group:CCI Solar Fuels
Funders:
Funding AgencyGrant Number
NIH 5 P41 RR001209
Department of Energy (DOE)UNSPECIFIED
NIHDK019038
Stanford Global Climate and Energy Project (GCEP)UNSPECIFIED
NSFCHE-0802907
Gordon and Betty Moore FoundationUNSPECIFIED
Subject Keywords:Chemical biology ; Inorganic chemistry
Issue or Number:9
PubMed Central ID:PMC2841405
Record Number:CaltechAUTHORS:20100107-092654651
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20100107-092654651
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:17086
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:11 Jan 2010 23:42
Last Modified:03 Oct 2019 01:22

Repository Staff Only: item control page