Structure of the binuclear heme iron-copper site in the quinol-oxidizing cytochrome aa3 from Bacillus subtilis

Linda S Powers, Marko Lauraeus, Konda S. Reddy, Britton Chance, Mårten Wikström

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Cytochrome aa3-600 is a terminal quinol oxidase of Bacillus subtilis, belonging to the large family of structurally and functionally related respiratory enzymes to which the mitochondrial cytochrome c oxidase also belongs. However, the CuA center typical of the cytochrome c oxidases is lacking from cytochrome aa3-600. The presence of only one copper, viz. CuB of the binuclear heme iron-copper site, makes cytochrome aa3-600 especially suitable for XAS analysis of this structure. Cu and Fe XAS data for fully oxidized cytochrome aa3-600 indicate a structure for the binuclear site similar to that previously reported for mitochondrial cytochrome c oxidase (see Powers et al. (1981) Biophys. J. 34, 465-468). Heme Fea3 has a proximal histidine nitrogen ligand 2.10 ± 0.02 A ̊ from the iron, and a distal S or Cl ligand at 2.36 ± 0.03 A ̊. The latter is also a ligand of CuB (2.21 ± 0.02 A ̊), and apparently forms a bridge between the two metals which are 3.70 ± 0.06 A ̊ apart. CuB has two more close-lying ligands at 1.95 ± 0.02 A ̊, which are likely histidine nitrogens. The similarity between EXAFS of CuB and type 1 'blue' copper is contrasted to EPR and optical spectroscopic properties of CuB, and the nature of the bridging ligand is discussed.

Original languageEnglish (US)
Pages (from-to)504-512
Number of pages9
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1183
Issue number3
DOIs
StatePublished - Jan 4 1994
Externally publishedYes

Fingerprint

Hydroquinones
Electron Transport Complex IV
Bacilli
Bacillus subtilis
Heme
Copper
Iron
Ligands
Histidine
Nitrogen
Paramagnetic resonance
Metals
Enzymes

Keywords

  • Cytochrome oxidase
  • EXAFS
  • Heme
  • Quinol oxidase

ASJC Scopus subject areas

  • Biophysics

Cite this

Structure of the binuclear heme iron-copper site in the quinol-oxidizing cytochrome aa3 from Bacillus subtilis. / Powers, Linda S; Lauraeus, Marko; Reddy, Konda S.; Chance, Britton; Wikström, Mårten.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1183, No. 3, 04.01.1994, p. 504-512.

Research output: Contribution to journalArticle

Powers, Linda S ; Lauraeus, Marko ; Reddy, Konda S. ; Chance, Britton ; Wikström, Mårten. / Structure of the binuclear heme iron-copper site in the quinol-oxidizing cytochrome aa3 from Bacillus subtilis. In: Biochimica et Biophysica Acta - Bioenergetics. 1994 ; Vol. 1183, No. 3. pp. 504-512.
@article{6262223f382a4d70a8e9b2225cf6e875,
title = "Structure of the binuclear heme iron-copper site in the quinol-oxidizing cytochrome aa3 from Bacillus subtilis",
abstract = "Cytochrome aa3-600 is a terminal quinol oxidase of Bacillus subtilis, belonging to the large family of structurally and functionally related respiratory enzymes to which the mitochondrial cytochrome c oxidase also belongs. However, the CuA center typical of the cytochrome c oxidases is lacking from cytochrome aa3-600. The presence of only one copper, viz. CuB of the binuclear heme iron-copper site, makes cytochrome aa3-600 especially suitable for XAS analysis of this structure. Cu and Fe XAS data for fully oxidized cytochrome aa3-600 indicate a structure for the binuclear site similar to that previously reported for mitochondrial cytochrome c oxidase (see Powers et al. (1981) Biophys. J. 34, 465-468). Heme Fea3 has a proximal histidine nitrogen ligand 2.10 ± 0.02 A ̊ from the iron, and a distal S or Cl ligand at 2.36 ± 0.03 A ̊. The latter is also a ligand of CuB (2.21 ± 0.02 A ̊), and apparently forms a bridge between the two metals which are 3.70 ± 0.06 A ̊ apart. CuB has two more close-lying ligands at 1.95 ± 0.02 A ̊, which are likely histidine nitrogens. The similarity between EXAFS of CuB and type 1 'blue' copper is contrasted to EPR and optical spectroscopic properties of CuB, and the nature of the bridging ligand is discussed.",
keywords = "Cytochrome oxidase, EXAFS, Heme, Quinol oxidase",
author = "Powers, {Linda S} and Marko Lauraeus and Reddy, {Konda S.} and Britton Chance and M{\aa}rten Wikstr{\"o}m",
year = "1994",
month = "1",
day = "4",
doi = "10.1016/0005-2728(94)90078-7",
language = "English (US)",
volume = "1183",
pages = "504--512",
journal = "Biochimica et Biophysica Acta - Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Structure of the binuclear heme iron-copper site in the quinol-oxidizing cytochrome aa3 from Bacillus subtilis

AU - Powers, Linda S

AU - Lauraeus, Marko

AU - Reddy, Konda S.

AU - Chance, Britton

AU - Wikström, Mårten

PY - 1994/1/4

Y1 - 1994/1/4

N2 - Cytochrome aa3-600 is a terminal quinol oxidase of Bacillus subtilis, belonging to the large family of structurally and functionally related respiratory enzymes to which the mitochondrial cytochrome c oxidase also belongs. However, the CuA center typical of the cytochrome c oxidases is lacking from cytochrome aa3-600. The presence of only one copper, viz. CuB of the binuclear heme iron-copper site, makes cytochrome aa3-600 especially suitable for XAS analysis of this structure. Cu and Fe XAS data for fully oxidized cytochrome aa3-600 indicate a structure for the binuclear site similar to that previously reported for mitochondrial cytochrome c oxidase (see Powers et al. (1981) Biophys. J. 34, 465-468). Heme Fea3 has a proximal histidine nitrogen ligand 2.10 ± 0.02 A ̊ from the iron, and a distal S or Cl ligand at 2.36 ± 0.03 A ̊. The latter is also a ligand of CuB (2.21 ± 0.02 A ̊), and apparently forms a bridge between the two metals which are 3.70 ± 0.06 A ̊ apart. CuB has two more close-lying ligands at 1.95 ± 0.02 A ̊, which are likely histidine nitrogens. The similarity between EXAFS of CuB and type 1 'blue' copper is contrasted to EPR and optical spectroscopic properties of CuB, and the nature of the bridging ligand is discussed.

AB - Cytochrome aa3-600 is a terminal quinol oxidase of Bacillus subtilis, belonging to the large family of structurally and functionally related respiratory enzymes to which the mitochondrial cytochrome c oxidase also belongs. However, the CuA center typical of the cytochrome c oxidases is lacking from cytochrome aa3-600. The presence of only one copper, viz. CuB of the binuclear heme iron-copper site, makes cytochrome aa3-600 especially suitable for XAS analysis of this structure. Cu and Fe XAS data for fully oxidized cytochrome aa3-600 indicate a structure for the binuclear site similar to that previously reported for mitochondrial cytochrome c oxidase (see Powers et al. (1981) Biophys. J. 34, 465-468). Heme Fea3 has a proximal histidine nitrogen ligand 2.10 ± 0.02 A ̊ from the iron, and a distal S or Cl ligand at 2.36 ± 0.03 A ̊. The latter is also a ligand of CuB (2.21 ± 0.02 A ̊), and apparently forms a bridge between the two metals which are 3.70 ± 0.06 A ̊ apart. CuB has two more close-lying ligands at 1.95 ± 0.02 A ̊, which are likely histidine nitrogens. The similarity between EXAFS of CuB and type 1 'blue' copper is contrasted to EPR and optical spectroscopic properties of CuB, and the nature of the bridging ligand is discussed.

KW - Cytochrome oxidase

KW - EXAFS

KW - Heme

KW - Quinol oxidase

UR - http://www.scopus.com/inward/record.url?scp=0028040080&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028040080&partnerID=8YFLogxK

U2 - 10.1016/0005-2728(94)90078-7

DO - 10.1016/0005-2728(94)90078-7

M3 - Article

C2 - 8286399

AN - SCOPUS:0028040080

VL - 1183

SP - 504

EP - 512

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

SN - 0005-2728

IS - 3

ER -