page_title: Hemocyanin
hierarchical_section_title: Hemocyanin
caption_attribution_description: Rendering of the molecular structure of a functional unit of octopus hemocyanin. From en:, created by en:User:BerserkerBen. Original text: Image I generated from .cn3 file upload from public access at https://www.ncbi.nlm.nih.gov/Structure/pdb/1JS8.
context_page_description: Hemocyanins are proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule. They are second only to hemoglobin in frequency of use as an oxygen transport molecule. Unlike the hemoglobin in red blood cells found in vertebrates, hemocyanins are not bound to blood cells but are instead suspended directly in the hemolymph. Oxygenation causes a color change between the colorless Cu(I) deoxygenated form and the blue Cu(II) oxygenated form.
context_section_description: Hemocyanins (also spelled haemocyanins and abbreviated Hc) are  proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule (O₂). They are second only to hemoglobin in frequency of use as an oxygen transport molecule. Unlike the hemoglobin in red blood cells found in vertebrates, hemocyanins are not bound to blood cells but are instead suspended directly in the hemolymph. Oxygenation causes a color change between the colorless Cu(I) deoxygenated form and the blue Cu(II) oxygenated form.
caption: Single oxygenated functional unit from the hemocyanin of an octopus
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