PMID- 11278308
OWN - NLM
STAT- MEDLINE
DCOM- 20010614
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 276
IP  - 17
DP  - 2001 Apr 27
TI  - Anesthetic-like interactions of nitric oxide with albumin and hemeproteins. A 
      mechanism for control of protein function.
PG  - 13635-43
AB  - Noncovalent bonding interactions of nitric oxide (NO) with human serum albumin 
      (HSA), human hemoglobin A, bovine myoglobin, and bovine cytochrome c oxidase 
      (CcO) have been explored. The anesthetic nitrous oxide (NNO) occupies multiple 
      sites within each protein, but does not bind to heme iron. Infrared (IR) spectra 
      of NNO molecules sequestered within albumin, with NO present, support the binding 
      of NO and NNO to the same sites with comparable affinities. Perturbations of IR 
      spectra of the Cys(34) thiol of HSA indicate NO, NNO, halothane, and chloroform 
      can induce similar changes in protein structure. Experiments evaluating the 
      relative affinities of binding of NO and carbon monoxide (CO) to iron(II) sites 
      of the hemeproteins led to evidence of NO binding to noniron, nonsulfur sites as 
      well. With HbA, IR spectra of cysteine thiols and/or the iron(II) N-O stretching 
      region denote changes in protein structure due to NO, NNO, or CO occupying 
      noniron sites with an order of decreasing affinities of NO > NNO > CO. Loss of NO 
      from some, not all, noniron sites in hemeproteins is very slow (t(1/2) 
      approximately hours). These findings provide examples in which NO and anesthetics 
      alter the structure and properties of protein similarly, and support the 
      hypothesis that some physiological effects of NO (and possibly CO) result from 
      anesthetic-like noncovalent bonding to sites within protein or other tissue 
      components. Such bonding may be involved in mechanisms for control of oxygen 
      transport, mitochondrial respiration, and activation of soluble guanylate cyclase 
      by NO.
FAU - Sampath, V
AU  - Sampath V
AD  - Department of Biochemistry and Molecular Biology, Colorado State University, Fort 
      Collins, Colorado 80523, USA.
FAU - Zhao, X J
AU  - Zhao XJ
FAU - Caughey, W S
AU  - Caughey WS
LA  - eng
GR  - HL-15890/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20010126
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Ligands)
RN  - 0 (Myoglobin)
RN  - 0 (Serum Albumin)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - 7V31YC746X (Chloroform)
RN  - 9034-51-9 (Hemoglobin A)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - EC 4.6.1.2 (Guanylate Cyclase)
RN  - S88TT14065 (Oxygen)
RN  - UQT9G45D1P (Halothane)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Chloroform/pharmacology
MH  - Electron Transport Complex IV/chemistry/*metabolism
MH  - Guanylate Cyclase/metabolism
MH  - Halothane/pharmacology
MH  - Hemoglobin A/chemistry/*metabolism
MH  - Humans
MH  - Ligands
MH  - Mitochondria/metabolism
MH  - Myoglobin/chemistry/*metabolism
MH  - Nitric Oxide/chemistry/*metabolism
MH  - Oxygen/metabolism
MH  - Protein Binding
MH  - Serum Albumin/chemistry/*metabolism
MH  - Spectrophotometry, Infrared
MH  - Time Factors
EDAT- 2001/03/30 10:00
MHDA- 2001/06/15 10:01
CRDT- 2001/03/30 10:00
PHST- 2001/03/30 10:00 [pubmed]
PHST- 2001/06/15 10:01 [medline]
PHST- 2001/03/30 10:00 [entrez]
AID - S0021-9258(20)78802-2 [pii]
AID - 10.1074/jbc.M006588200 [doi]
PST - ppublish
SO  - J Biol Chem. 2001 Apr 27;276(17):13635-43. doi: 10.1074/jbc.M006588200. Epub 2001 
      Jan 26.