Metalloproteins

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 confined in 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) oxygen

thumb|right|The structure of hemoglobin. The [[heme cofactor, containing the metal iron, shown in green.]]

class of enzymes

class of enzymes

Photosystems are functional and structural units of protein complexes involved in photosynthesis. Together they carry out the primary photochemistry of photosynthesis: the absorption of light and the transfer of energy and electrons. Photosystems are found in the thylakoid membranes of plants, algae, and cyanobacteria. These membranes are located inside the chloroplasts of plants and algae, and in the cytoplasmic membrane of photosynthetic bacteria. There are two kinds of photosystems: PSI and PSII. center|thumb|650x650px|Model of a photosystem and how it uses light energy to carry out process

thumb|right|Trimeric Hemerythrin Protein Complex () Hemerythrin (also spelled haemerythrin; , ) is an oligomeric protein responsible for oxygen (O2) transport in the marine invertebrate phyla of priapulids, brachiopods, and in the annelid worm clades Magelona and Sipuncula. Myohemerythrin is a monomeric O2-binding protein found in the muscles of marine invertebrates. Hemerythrin and myohemerythrin are essentially colorless when deoxygenated, but turn a violet-pink in the oxygenated state.

family of zinc-dependent metalloendopeptidases that is involved in the degradation of the extracellular matrix

mammalian protein found in Homo sapiens

class of proteins in which iron is coordinated with cysteine sulfur and also with inorganic sulfur

class of enzymes

Superoxide dismutase [Cu-Zn] also known as superoxide dismutase 1 or hSod1 is an enzyme that in humans is encoded by the SOD1 gene, located on chromosome 21. SOD1 is one of three human superoxide dismutases. It is implicated in apoptosis, familial amyotrophic lateral sclerosis and Parkinson's disease.

right|thumb|Sea squirt ([[Didemnum molle) off Sulawesi, Indonesia]] Hemovanadin is a pale green vanabin protein found in the blood cells, called vanadocytes, of ascidians (sea squirts) and other organisms (particularly sea organisms). It is one of the few known vanadium-containing proteins. The German chemist Martin Henze first detected vanadium in ascidians (sea squirts) in 1911. Unlike hemocyanin and hemoglobin, hemovanadin is not an oxygen carrier.

protein-coding gene in the species Homo sapiens

Rubredoxins are a class of low-molecular-weight iron-containing proteins found in sulfur-metabolizing bacteria and archaea. Sometimes rubredoxins are classified as iron-sulfur proteins; however, in contrast to iron-sulfur proteins, rubredoxins do not contain inorganic sulfide. Like cytochromes, ferredoxins and Rieske proteins, rubredoxins are thought to participate in electron transfer in biological systems. Recent work in bacteria and algae have led to the hypothesis that some rubredoxins may instead have a role in delivering iron to metalloproteins.

thumb|3-D representation of the structure of Vanabin2 from Ascisia sydneiensis var. samea

protein family

Superoxide dismutase 2, mitochondrial (SOD2), also known as manganese-dependent superoxide dismutase (MnSOD), is an enzyme which in humans is encoded by the SOD2 gene on chromosome 6. A related pseudogene has been identified on chromosome 1. Alternative splicing of this gene results in multiple transcript variants. This gene is a member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen p