The Reaction of Helix pomatia Methaemocyanin with Azide and Flouride-Reference-Cited by-同舟云学术

The Reaction of Helix pomatia Methaemocyanin with Azide and Flouride

Published:1977 Issue: Volume: Page:239-244
ISSN:0172-6625
Container-title:Proceedings in Life Sciences
language:
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Author:

Witters R.,De Ley M.,Lontie R.

Publisher

Springer Berlin Heidelberg

Link

http://link.springer.com/content/pdf/10.1007/978-3-642-66679-7_30

Reference10 articles.

1. Byers, W., Curzon, G., Garbett, K., Speyer, B.E., Young, S.N., Williams, R.J.P.: Anion-binding and the state of copper in caeruloplasmin. Biochem. Biophys. Acta 310, 38–50 (1973)

2. De Ley, M., Candreva, F., Witters, R., Lontie, R.: The fast reduction of Helix pomatia methaemocyanin with hydrogen sulphide. FEBS Lett. 57, 234–236 (1975)

3. Dunhill, R.H., Pilbrow, J.R., Smith, T.D.: Electron spin resonance of copper(II) citrate chelates. J. Chem. Phys. 45, 1474–1481 (1966)

4. Guillemet, R., Gosselin, G.: Sur les rapports entre le cuivre et la capacite’ respi- ratoire dans les sangs hemocyaniques. Compt. Rend. Soc. Biol. 1ll, 733–735 (1932)

5. Heirwegh, K., Lontie, R.: Decrease of the copper bands of Helix pomatia haemocyanin. Nature (London) .185, 854–855 (1960)

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1. The Reaction of Nitrogen Monoxide and of Nitrite with Deoxyhaemocyanin and Methaemocyanin of Helix pomatia;European Journal of Biochemistry;1979-04

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3. Metal-metal interactions in metalloporphyrins, metalloproteins and metalloenzymes;Structure and Bonding

4. Active sites in copper proteins an electronic structure overview;Copper, Molybdenum, and Vanadium in Biological Systems