3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin

Gaykema, W. P. J.; Hól, Wim G. J.; Vereijken, J.M.; Soeter, Nell M.; Bak, Henk J.; Beintema, Jaap J.

doi:10.1038/309023a0

Cited by 359 publications

(194 citation statements)

References 52 publications

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“…From a crystallographic analysis of Palinurus interruptus haemocyanin [31], one of the pair of copper ions, Cu(A), is surrounded by residues 196, 200 and 226 ; the other, Cu(B), is surrounded by residues 346, 350 and 386. Mutation positions were selected on the basis of a sequence comparison of the tyrosinase from A. oryzae [7] with other tyrosinases from N. crassa [8][9][10][11], S. antibioticus [13] and H. sapiens [12] (Figure 2).…”

Section: Resultsmentioning

confidence: 99%

Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis

et al. 2000

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Section: Resultsmentioning

confidence: 99%

Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis

et al. 2000

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“…Arthropod hemocyanins form hexamers or oligo-hexamers from several paralogus subunit types, which possess three distinct domains. Each subunit bears a single active site and has a molecular mass of 75 kDa (5,15). In contrast, mollusc hemocyanins form hollow cylinders made up from 10 copies of the same subunit type.…”

Section: Introductionmentioning

confidence: 99%

“…As type 3 copper proteins and their active sites are embedded in a four a-helix bundle with six histidine residues, which coordinate two copper atoms (4)(5)(6)(7)(8). Between them one molecule oxygen is reversibly bound in side-on (l-g 2 :g 2 ) coordination (4,7,9,10).…”

Section: Introductionmentioning

confidence: 99%

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The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1‐h) reveals disulfide bridges

et al. 2011

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Hemocyanins are multimeric oxygen‐transport proteins in the hemolymph of many arthropods and mollusks. The overall molecular architecture of arthropod and molluscan hemocyanin is very different, although they possess a similar binuclear type 3 copper center to bind oxygen in a side‐on conformation. Gastropod hemocyanin is a 35 nm cylindrical didecamer (2 × 10‐mer) based on a 400 kDa subunit. The latter is subdivided into eight paralogous “functional units” (FU‐a to FU‐h), each with an active site. FU‐a to FU‐f contribute to the cylinder wall, whereas FU‐g and FU‐h form the internal collar complex. Atomic structures of FU‐e and FU‐g, and a 9 Å cryoEM structure of the 8 MDa didecamer are available. Recently, the structure of keyhole limpet hemocyanin FU‐h (KLH1‐h) was presented as a Cα‐trace at 4 Å resolution. Unlike the other seven FU types, FU‐h contains an additional C‐terminal domain with a cupredoxin‐like fold. Because of the resolution limit of 4 Å, in some loops, the course of the protein backbone could not be established with high certainty yet. Here, we present a refined atomic structure of FU‐h (KLH1‐h) obtained from low‐resolution refinement, which unambiguously establishes the course of the polypeptide backbone and reveals the disulfide bridges as well as the orientation of bulky amino acids. © 2011 IUBMB IUBMB Life, 63(3): 183–187, 2011

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“…1) elles sont principalement considérées comme transporteurs d'oxygène dans l'hémolymphe d'arthropodes et de mollusques. Il est généra-lement admis que dans le site actif, chaque cation cuivre est relié à trois résidus imidazole d'histidine [13], le quatrième ligand, endogène, est constitué par un phénolate, le cinquième, exogène, provient de l'oxygène (sous forme d'un pont peroxyde) [8,11,19,22]. Il a déjà été montré que cette protéine possède des activités peroxydasiques [17] ainsi qu'une activité catalasique [12,15,21,30].…”

Section: Introductionunclassified

Étude cinétique des propriétés catalytiques de l’hémocyanine de scorpion

Quéinnec

Gardès-Albert

Ducancel³

et al. 1991

J. Chim. Phys.

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RÉSUMÉLes hémocyanines, métalloprotéines à cuivre, ont pour fonction de transporter l'oxygène dissous dans l'hémolymphe de nombreux mollusques et arthropodes. L'oxyhémocyanine de scorpion présente également des propriétés enzymatiques remarquables : peroxydasiques et catalasiques, bien qu'elle ne possède ni fer, ni noyau porphyrinique. L'aspect cinétique de la réaction catalasique est ici décrite pour la première fois. La constante de vitesse de la réaction globale de l'eau oxygénée avec l'hémocyanine a été déterminée, elle est égale à (2,25 ± 0,25).10 4 moM.l.s -1 . Par ailleurs, une étude quantitative par radiolyse «puisée a permis de mettre en évidence la catalyse de la dismutation de l'anion superoxyde par l'hémocyanine à pH 9. La valeur de la constante de vitesse de cette réaction est égale à 3,5.10 7 mol -1 .l.s _1 . SUMMARYHemocyanins are copper proteins which function as oxygen carriers in thé haemolymph of molluscs and arthropods. Scorpion's oxyhemocyanin has enzymatic properties : peroxidasic and catalasic activities, although it has neither iron nor porphyrin ring in the active site. The kinetics of the catalasic reaction is described for the first time and the rate constant of the reaction is (2.25 ± 0.25) x 10 4 moM.l.s" 1 . The reaction of superoxide anion with hemocyanin has been studied using pulse radiolysis at pH 9. The catalytic rate constant is 3.5. x 10 7 moM.l.s" 1 .

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3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin

Cited by 359 publications

References 52 publications

Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis

Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis

The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1‐h) reveals disulfide bridges

Étude cinétique des propriétés catalytiques de l’hémocyanine de scorpion

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