| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print March 29, 2005
Okazaki Institute for Integrative Bioscience, Okazaki, Aichi 444-8787
Corresponding Author: uchida{at}ims.ac.jp
Neuronal PAS domain protein 2, which was recently established to be a heme protein, acts as a CO-dependent transcription factor. The protein consists of the basic helix-loop-helix domain, and two heme-containing PAS domains (PAS-A and PAS-B). In this study, we prepared wild-type and mutants of the isolated PAS-A domain, and measured resonance Raman spectra of these proteins. Upon excitation of the Raman spectrum at 363.8 nm, a band assignable to Fe3+-S stretching was observed at 334 cm-1 for the ferric wild-type protein; in contrast, this band was drastically weaker in the spectrum of C170A, suggesting that Cys170 is an axial ligand of the ferric heme. The Raman spectrum of the reduced form of wild-type was mainly of 6-coordinate low-spin, and the
J. Biol. Chem, 10.1074/jbc.M412350200
Submitted on November 1, 2004
Revised on March 16, 2005
Accepted on March 29, 2005
CO-dependent activity controlling mechanism of Heme-containing CO-sensor protein, NPAS2
11 band, which is sensitive to the donor strength of the axial ligand, was lower than that of reduced cytochrome c3, suggesting coordination of a strong ligand, and thus a deprotonated His. In the reduced forms of H119A and H171A, the 5-coordinate species became more prevalent, whereas no such changes were observed for C170A, indicating that His119 and His171, but not Cys170, are axial ligands in the ferrous heme. This means that ligand replacement from Cys to His occurs upon heme reduction. The Fe-CO vs C-O correlation indicates that a neutral His is a trans ligand of CO. Our results support a mechanism in which CO binding disrupts the hydrogen bonding of His171 with surrounding amino acids, which induces conformational changes in the His171-Cys170 moiety, leading to physiological signaling.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  R. L. Kerby, H. Youn, and G. P. Roberts RcoM: A New Single-Component Transcriptional Regulator of CO Metabolism in Bacteria J. Bacteriol., May 1, 2008; 190(9): 3336 - 3343. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Lu, M. Mukai, Y. Lin, G. Wu, R. K. Poole, and S.-R. Yeh Structural and Functional Properties of a Single Domain Hemoglobin from the Food-borne Pathogen Campylobactor jejuni J. Biol. Chem., August 31, 2007; 282(35): 25917 - 25928. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. M. Leu, N. J. Silvernail, M. Z. Zgierski, G. R. A. Wyllie, M. K. Ellison, W. R. Scheidt, J. Zhao, W. Sturhahn, E. E. Alp, and J. T. Sage Quantitative Vibrational Dynamics of Iron in Carbonyl Porphyrins Biophys. J., June 1, 2007; 92(11): 3764 - 3783. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Ibrahim, R. L. Kerby, M. Puranik, I. H. Wasbotten, H. Youn, G. P. Roberts, and T. G. Spiro Heme Displacement Mechanism of CooA Activation: MUTATIONAL AND RAMAN SPECTROSCOPIC EVIDENCE J. Biol. Chem., September 29, 2006; 281(39): 29165 - 29173. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
