PMID- 15811506
OWN - NLM
STAT- MEDLINE
DCOM- 20050613
LR  - 20131121
IS  - 0162-0134 (Print)
IS  - 0162-0134 (Linking)
VI  - 99
IP  - 4
DP  - 2005 Apr
TI  - Ligand specificity of H-NOX domains: from sGC to bacterial NO sensors.
PG  - 892-902
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. This family of heme proteins has been named the H-NOX 
      domain, for Heme-Nitric oxide/OXygen binding domain. The key observation from 
      initial studies in this family is that some members, those proteins from most 
      eukaryotes and facultative aerobic prokaryotes, bind NO in a five-coordinate heme 
      complex, but do not bind oxygen (O(2)), the same ligand binding characteristics 
      as sGC. H-NOX family members from obligate aerobic prokaryotes bind O(2) and NO 
      in six-coordinate complexes, similar to the globins and other O(2)-sensing heme 
      proteins. The molecular factors that contribute to these differences in ligand 
      specificity, within a family of sequence related proteins, are the subject of 
      this review.
FAU - Boon, Elizabeth M
AU  - Boon EM
AD  - Department of Chemistry, Lawrence Berkeley National Laboratory, University of 
      California-Berkeley, Berkeley, CA 94705-1460, USA.
FAU - Marletta, Michael A
AU  - Marletta MA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - United States
TA  - J Inorg Biochem
JT  - Journal of inorganic biochemistry
JID - 7905788
RN  - 0 (Bacterial Proteins)
RN  - 0 (Ligands)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - 42VZT0U6YR (Heme)
RN  - EC 4.6.1.2 (Guanylate Cyclase)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bacterial Proteins/metabolism
MH  - *Biosensing Techniques
MH  - Drosophila/enzymology
MH  - Genomics
MH  - Guanylate Cyclase/chemistry/genetics/*metabolism
MH  - Heme/*chemistry
MH  - Ligands
MH  - Molecular Sequence Data
MH  - Nitric Oxide/*chemistry
MH  - Oxygen/chemistry
MH  - Prokaryotic Cells/metabolism
MH  - Protein Binding
MH  - Sequence Alignment
RF  - 81
EDAT- 2005/04/07 09:00
MHDA- 2005/06/14 09:00
CRDT- 2005/04/07 09:00
PHST- 2004/11/12 00:00 [received]
PHST- 2004/11/26 00:00 [revised]
PHST- 2004/12/17 00:00 [accepted]
PHST- 2005/04/07 09:00 [pubmed]
PHST- 2005/06/14 09:00 [medline]
PHST- 2005/04/07 09:00 [entrez]
AID - S0162-0134(04)00420-9 [pii]
AID - 10.1016/j.jinorgbio.2004.12.016 [doi]
PST - ppublish
SO  - J Inorg Biochem. 2005 Apr;99(4):892-902. doi: 10.1016/j.jinorgbio.2004.12.016.