PMID- 15287748
OWN - NLM
STAT- MEDLINE
DCOM- 20040930
LR  - 20161122
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 43
IP  - 31
DP  - 2004 Aug 10
TI  - Spectroscopic characterization of the soluble guanylate cyclase-like heme domains 
      from Vibrio cholerae and Thermoanaerobacter tengcongensis.
PG  - 10203-11
AB  - Soluble guanylate cyclase (sGC) is a nitric oxide- (NO-) sensing hemoprotein that 
      has been found in eukaryotes from Drosophila to humans. Prokaryotic proteins with 
      significant homology to the heme domain of sGC have recently been identified 
      through genomic analysis. Characterization of two of these proteins is reported 
      here. The first is a 181 amino acid protein cloned from Vibrio cholerae (VCA0720) 
      that is encoded in a histidine kinase-containing operon. The ferrous unligated 
      form of VCA0720 is 5-coordinate, high-spin. The CO complex is low-spin, 
      6-coordinate, and the NO complex is high-spin and 5-coordinate. These 
      ligand-binding properties are very similar to those of sGC. The second protein is 
      the N-terminal 188 amino acids of Tar4 (TtTar4H), a predicted methyl-accepting 
      chemotaxis protein (MCP) from the strict anaerobe Thermoanaerobacter 
      tengcongensis. TtTar4H forms a low-spin, 6-coordinate ferrous-oxy complex, the 
      first of this sGC-related family that binds O2. TtTar4H has ligand-binding 
      properties similar to those of the heme-containing O2 sensors such as AxPDEA1. 
      sGC does not bind O2 despite having a porphyrin with a histidyl ligand like the 
      globins. The results reported here, with sequence-related proteins from 
      prokaryotes but in the same family as the sGC heme domain, show that these 
      proteins have evolved to discriminate between ligands such as NO and O2; hence, 
      we term this family H-NOX domains (heme-nitric oxide/oxygen).
FAU - Karow, David S
AU  - Karow DS
AD  - Program in Cellular and Molecular Biology, University of Michigan, Ann Arbor, 
      Michigan 48109, USA.
FAU - Pan, Duohai
AU  - Pan D
FAU - Tran, Rosalie
AU  - Tran R
FAU - Pellicena, Patricia
AU  - Pellicena P
FAU - Presley, Andrew
AU  - Presley A
FAU - Mathies, Richard A
AU  - Mathies RA
FAU - Marletta, Michael A
AU  - Marletta MA
LA  - eng
GR  - F32 GM068262/GM/NIGMS NIH HHS/United States
GR  - F32 GM068262-01/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Bacterial Proteins)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Ferrous Compounds)
RN  - 0 (Ligands)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Tar protein, E coli)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - 42VZT0U6YR (Heme)
RN  - 7U1EE4V452 (Carbon Monoxide)
RN  - EC 4.6.1.2 (Guanylate Cyclase)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/*chemistry
MH  - Carbon Monoxide/chemistry
MH  - Chemoreceptor Cells
MH  - Cloning, Molecular
MH  - Clostridium/*enzymology
MH  - Escherichia coli Proteins
MH  - Ferrous Compounds/chemistry
MH  - Gene Expression Regulation, Bacterial
MH  - Guanylate Cyclase/*chemistry/genetics/isolation & purification
MH  - Heme/*chemistry
MH  - Ligands
MH  - Molecular Sequence Data
MH  - Nitric Oxide/chemistry
MH  - Oxygen/chemistry
MH  - Protein Structure, Tertiary
MH  - Receptors, Cell Surface
MH  - Solubility
MH  - Spectrophotometry, Ultraviolet
MH  - Spectrum Analysis, Raman
MH  - Vibrio cholerae/*enzymology
EDAT- 2004/08/04 05:00
MHDA- 2004/10/02 05:00
CRDT- 2004/08/04 05:00
PHST- 2004/08/04 05:00 [pubmed]
PHST- 2004/10/02 05:00 [medline]
PHST- 2004/08/04 05:00 [entrez]
AID - 10.1021/bi049374l [doi]
PST - ppublish
SO  - Biochemistry. 2004 Aug 10;43(31):10203-11. doi: 10.1021/bi049374l.