PMID- 15100039
OWN - NLM
STAT- MEDLINE
DCOM- 20040617
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1655
IP  - 1-3
DP  - 2004 Apr 12
TI  - The use of stable isotopes and spectroscopy to investigate the energy transducing 
      function of cytochrome c oxidase.
PG  - 248-55
AB  - We have used EPR and FTIR spectroscopy in combination with (17)O and (15)N stable 
      isotopes to investigate the mechanism of cytochrome c oxidase (CcO). A high-spin 
      state of heme a(3) was found in high yield by EPR, achieved upon turning over the 
      enzyme until it was anaerobic, and shown to be a mixture of heme with a 
      coordinated oxygen-based ligand and five-coordinate heme. Allowing the enzyme to 
      consume (17)O(2) for a few milliseconds before freezing, we also showed that the 
      product H(2)(17)O exits toward the external side of the enzyme, binding to the 
      nonredox active Mg/Mn site en route. Specific (15)N labeling of histidine, in 
      comparison with global (15)N labeling and unlabeled samples, allowed us to more 
      definitively assign heme and histidine peaks in the electrochemically induced 
      FTIR difference spectrum. Additionally, the assignment of heme bands affords a 
      reliable method of spectrum normalization between samples, providing a more 
      accurate comparison of the spectral features of bovine with bacterial cytochrome 
      oxidase and revealing multiple differences between the two species.
FAU - Schmidt, Bryan
AU  - Schmidt B
AD  - Department of Chemistry, Michigan State University, East Lansing MI 48824, USA.
FAU - Hillier, Warwick
AU  - Hillier W
FAU - McCracken, John
AU  - McCracken J
FAU - Ferguson-Miller, Shelagh
AU  - Ferguson-Miller S
LA  - eng
GR  - GM26916/GM/NIGMS NIH HHS/United States
GR  - GM25486/GM/NIGMS NIH HHS/United States
GR  - P01 GM57323/GM/NIGMS NIH HHS/United States
GR  - R01 GM026916/GM/NIGMS NIH HHS/United States
GR  - RR02231/RR/NCRR NIH HHS/United States
GR  - GM37300/GM/NIGMS NIH HHS/United States
GR  - GM54065/GM/NIGMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Nitrogen Isotopes)
RN  - 0 (Oxygen Isotopes)
RN  - 18535-39-2 (heme a)
RN  - 42VZT0U6YR (Heme)
RN  - 42Z2K6ZL8P (Manganese)
RN  - 4QD397987E (Histidine)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Electrochemistry
MH  - Electron Spin Resonance Spectroscopy
MH  - Electron Transport Complex IV/*chemistry/*metabolism
MH  - Energy Metabolism
MH  - Heme/*analogs & derivatives/chemistry
MH  - Histidine/chemistry
MH  - Manganese/chemistry
MH  - Models, Biological
MH  - Nitrogen Isotopes
MH  - Oxygen Isotopes
MH  - Rhodobacter sphaeroides/enzymology
MH  - Spectroscopy, Fourier Transform Infrared
RF  - 43
EDAT- 2004/04/22 05:00
MHDA- 2004/06/18 05:00
CRDT- 2004/04/22 05:00
PHST- 2003/04/23 00:00 [received]
PHST- 2003/11/05 00:00 [revised]
PHST- 2003/11/05 00:00 [accepted]
PHST- 2004/04/22 05:00 [pubmed]
PHST- 2004/06/18 05:00 [medline]
PHST- 2004/04/22 05:00 [entrez]
AID - S0005272803002184 [pii]
AID - 10.1016/j.bbabio.2003.11.008 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2004 Apr 12;1655(1-3):248-55. doi: 
      10.1016/j.bbabio.2003.11.008.