PMID- 32123230
OWN - NLM
STAT- MEDLINE
DCOM- 20201112
LR  - 20210302
IS  - 2045-2322 (Electronic)
IS  - 2045-2322 (Linking)
VI  - 10
IP  - 1
DP  - 2020 Mar 2
TI  - Characterisation of the Cyanate Inhibited State of Cytochrome c Oxidase.
PG  - 3863
LID - 10.1038/s41598-020-60801-0 [doi]
LID - 3863
AB  - Heme-copper oxygen reductases are terminal respiratory enzymes, catalyzing the 
      reduction of dioxygen to water and the translocation of protons across the 
      membrane. Oxygen consumption is inhibited by various substances. Here we tested 
      the relatively unknown inhibition of cytochrome c oxidase (CcO) with isocyanate. 
      In contrast to other more common inhibitors like cyanide, inhibition with cyanate 
      was accompanied with the rise of a metal to ligand charge transfer (MLCT) band 
      around 638 nm. Increasing the cyanate concentration furthermore caused selective 
      reduction of heme a. The presence of the CT band allowed for the first time to 
      directly monitor the nature of the ligand via surface-enhanced resonance Raman 
      (SERR) spectroscopy. Analysis of isotope sensitive SERR spectra in comparison 
      with Density Functional Theory (DFT) calculations identified not only the cyanate 
      monomer as an inhibiting ligand but suggested also presence of an uretdion ligand 
      formed upon dimerization of two cyanate ions. It is therefore proposed that under 
      high cyanate concentrations the catalytic site of CcO promotes cyanate 
      dimerization. The two excess electrons that are supplied from the uretdion ligand 
      lead to the observed physiologically inverse electron transfer from heme a(3) to 
      heme a.
FAU - Kruse, Fabian
AU  - Kruse F
AD  - Technische Universitat Dresden, Department of Chemistry and Food Chemistry, 
      01069, Dresden, Germany.
FAU - Nguyen, Anh Duc
AU  - Nguyen AD
AD  - Technische Universitat Berlin, Department of Chemistry, Strasse des 17. Juni 135, 
      10623, Berlin, Germany.
FAU - Dragelj, Jovan
AU  - Dragelj J
AD  - Technische Universitat Berlin, Department of Chemistry, Strasse des 17. Juni 135, 
      10623, Berlin, Germany.
FAU - Schlesinger, Ramona
AU  - Schlesinger R
AUID- ORCID: 0000-0002-7716-4439
AD  - Freie Universitat Berlin, Department of Physics, Arnimallee 14, 14195, Berlin, 
      Germany.
FAU - Heberle, Joachim
AU  - Heberle J
AD  - Freie Universitat Berlin, Department of Physics, Arnimallee 14, 14195, Berlin, 
      Germany.
FAU - Mroginski, Maria Andrea
AU  - Mroginski MA
AUID- ORCID: 0000-0002-7497-5631
AD  - Technische Universitat Berlin, Department of Chemistry, Strasse des 17. Juni 135, 
      10623, Berlin, Germany.
FAU - Weidinger, Inez M
AU  - Weidinger IM
AUID- ORCID: 0000-0001-9316-6349
AD  - Technische Universitat Dresden, Department of Chemistry and Food Chemistry, 
      01069, Dresden, Germany. inez.weidinger@tu-dresden.de.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20200302
PL  - England
TA  - Sci Rep
JT  - Scientific reports
JID - 101563288
RN  - 0 (Bacterial Proteins)
RN  - 0 (Cyanates)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
EIN - Sci Rep. 2020 Apr 17;10(1):6853. PMID: 32300182
MH  - Bacterial Proteins/*chemistry
MH  - Catalytic Domain
MH  - Cyanates/*chemistry
MH  - Electron Transport Complex IV/*chemistry
MH  - Rhodobacter sphaeroides/*enzymology
PMC - PMC7052191
COIS- The authors declare no competing interests.
EDAT- 2020/03/04 06:00
MHDA- 2020/11/13 06:00
PMCR- 2020/03/02
CRDT- 2020/03/04 06:00
PHST- 2019/03/22 00:00 [received]
PHST- 2020/02/17 00:00 [accepted]
PHST- 2020/03/04 06:00 [entrez]
PHST- 2020/03/04 06:00 [pubmed]
PHST- 2020/11/13 06:00 [medline]
PHST- 2020/03/02 00:00 [pmc-release]
AID - 10.1038/s41598-020-60801-0 [pii]
AID - 60801 [pii]
AID - 10.1038/s41598-020-60801-0 [doi]
PST - epublish
SO  - Sci Rep. 2020 Mar 2;10(1):3863. doi: 10.1038/s41598-020-60801-0.