Structural model of the redox centres in cytochrome oxidase

Liisa Holm, Matti Saraste, Mårten Wikström

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Evolutionary conservation, predicted membrane topography of the subunits, and known chemical and physical properties of the catalytic metals in cytochrome oxidase provided the basis for plausible structural models of the enzyme's redox centres.
Subunit II probably binds one of the copper ions (CuA) whilst subunit I is likely to bind the two haems (a and a3) and the other redox‐active copper (CuB). Two cysteine and two histidine residues of subunit II are the likely ligands of CuA, forming a centre that may be structurally similar to that in azurin. The two haems may be sandwiched between two transmembranous segments of subunit I, one of which also provides a histidine ligand to CuB. A third segment may provide two more histidine ligands to the latter.
The model was constructed with a 4 A Fe‐Cu distance in the binuclear haem a3‐CuB centre, and a 14 A distance between the haem irons.
The subunit I model involves only three transmembranous helices which bind three catalytic metal groups. The fit of this model to several known physicochemical properties of the redox centres is analysed.
Original languageEnglish
Pages (from-to)2819-2823
JournalEMBO Journal
Volume6
Issue number9
DOIs
Publication statusPublished - 1987
MoE publication typeA1 Journal article-refereed

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Structural Models
Electron Transport Complex IV
Heme
Oxidation-Reduction
Histidine
Ligands
Copper
Azurin
Metals
Topography
Chemical properties
Cysteine
Conservation
Physical properties
Ions
Iron
Membranes
Enzymes

Cite this

Holm, Liisa ; Saraste, Matti ; Wikström, Mårten. / Structural model of the redox centres in cytochrome oxidase. In: EMBO Journal. 1987 ; Vol. 6, No. 9. pp. 2819-2823.
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abstract = "Evolutionary conservation, predicted membrane topography of the subunits, and known chemical and physical properties of the catalytic metals in cytochrome oxidase provided the basis for plausible structural models of the enzyme's redox centres. Subunit II probably binds one of the copper ions (CuA) whilst subunit I is likely to bind the two haems (a and a3) and the other redox‐active copper (CuB). Two cysteine and two histidine residues of subunit II are the likely ligands of CuA, forming a centre that may be structurally similar to that in azurin. The two haems may be sandwiched between two transmembranous segments of subunit I, one of which also provides a histidine ligand to CuB. A third segment may provide two more histidine ligands to the latter. The model was constructed with a 4 A Fe‐Cu distance in the binuclear haem a3‐CuB centre, and a 14 A distance between the haem irons. The subunit I model involves only three transmembranous helices which bind three catalytic metal groups. The fit of this model to several known physicochemical properties of the redox centres is analysed.",
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Structural model of the redox centres in cytochrome oxidase. / Holm, Liisa; Saraste, Matti; Wikström, Mårten.

In: EMBO Journal, Vol. 6, No. 9, 1987, p. 2819-2823.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Structural model of the redox centres in cytochrome oxidase

AU - Holm, Liisa

AU - Saraste, Matti

AU - Wikström, Mårten

PY - 1987

Y1 - 1987

N2 - Evolutionary conservation, predicted membrane topography of the subunits, and known chemical and physical properties of the catalytic metals in cytochrome oxidase provided the basis for plausible structural models of the enzyme's redox centres. Subunit II probably binds one of the copper ions (CuA) whilst subunit I is likely to bind the two haems (a and a3) and the other redox‐active copper (CuB). Two cysteine and two histidine residues of subunit II are the likely ligands of CuA, forming a centre that may be structurally similar to that in azurin. The two haems may be sandwiched between two transmembranous segments of subunit I, one of which also provides a histidine ligand to CuB. A third segment may provide two more histidine ligands to the latter. The model was constructed with a 4 A Fe‐Cu distance in the binuclear haem a3‐CuB centre, and a 14 A distance between the haem irons. The subunit I model involves only three transmembranous helices which bind three catalytic metal groups. The fit of this model to several known physicochemical properties of the redox centres is analysed.

AB - Evolutionary conservation, predicted membrane topography of the subunits, and known chemical and physical properties of the catalytic metals in cytochrome oxidase provided the basis for plausible structural models of the enzyme's redox centres. Subunit II probably binds one of the copper ions (CuA) whilst subunit I is likely to bind the two haems (a and a3) and the other redox‐active copper (CuB). Two cysteine and two histidine residues of subunit II are the likely ligands of CuA, forming a centre that may be structurally similar to that in azurin. The two haems may be sandwiched between two transmembranous segments of subunit I, one of which also provides a histidine ligand to CuB. A third segment may provide two more histidine ligands to the latter. The model was constructed with a 4 A Fe‐Cu distance in the binuclear haem a3‐CuB centre, and a 14 A distance between the haem irons. The subunit I model involves only three transmembranous helices which bind three catalytic metal groups. The fit of this model to several known physicochemical properties of the redox centres is analysed.

U2 - 10.1002/j.1460-2075.1987.tb02578.x

DO - 10.1002/j.1460-2075.1987.tb02578.x

M3 - Article

VL - 6

SP - 2819

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JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 9

ER -