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  2. Iron–sulfur protein - Wikipedia

    en.wikipedia.org/wiki/Iron–sulfur_protein

    Iron–sulfur proteins are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins , such as the ferredoxins , as well as NADH dehydrogenase , hydrogenases , coenzyme Q – cytochrome ...

  3. Succinylation - Wikipedia

    en.wikipedia.org/wiki/Succinylation

    The potential role of succinylation is under investigation, but as addition of succinyl group changes lysine's charge from +1 to −1 (at physiological pH) and introduces a relatively large structural moiety (100 Da), bigger than acetylation (42 Da) or methylation (14 Da), it is expected to lead to more significant changes in protein structure ...

  4. Ribbon diagram - Wikipedia

    en.wikipedia.org/wiki/Ribbon_diagram

    Ribbon diagram of myoglobin bound to haem (sticks) and oxygen (red spheres) (Ribbon diagrams, also known as Richardson diagrams, are 3D schematic representations of protein structure and are one of the most common methods of protein depiction used today. The ribbon depicts the general course and organisation of the protein backbone in 3D and ...

  5. Iron–sulfur cluster - Wikipedia

    en.wikipedia.org/wiki/Iron–sulfur_cluster

    Iron–sulfur clusters are molecular ensembles of iron and sulfide. They are most often discussed in the context of the biological role for iron–sulfur proteins , which are pervasive. [ 2 ] Many Fe–S clusters are known in the area of organometallic chemistry and as precursors to synthetic analogues of the biological clusters.

  6. Iron–sulfur cluster biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Iron–sulfur_cluster...

    The iron sulfur proteins contain iron–sulfur clusters, some with elaborate structures, that feature iron and sulfide centers. One broad biosynthetic task is producing sulfide (S 2-), which requires various families of enzymes. Another broad task is affixing the sulfide to iron, which is achieved on scaffolds, which are nonfunctional.

  7. SDHB - Wikipedia

    en.wikipedia.org/wiki/SDHB

    The expressed protein weighs 31.6 kDa and is composed of 280 amino acids. [ 8 ] [ 9 ] SDHB contains the iron-sulphur clusters necessary for tunneling electrons through the complex. It is located between SDHA and the two transmembrane subunits SDHC and SDHD .

  8. Iron in biology - Wikipedia

    en.wikipedia.org/wiki/Iron_in_biology

    Iron is also stored as a pigment called hemosiderin, which is an ill-defined deposit of protein and iron, created by macrophages where excess iron is present, either locally or systemically, e.g., among people with iron overload due to frequent blood cell destruction and the necessary transfusions their condition calls for. If systemic iron ...

  9. Category:Iron–sulfur proteins - Wikipedia

    en.wikipedia.org/wiki/Category:Iron–sulfur...

    Iron–sulfur proteins are proteins characterized by the presence of polymetallic systems (iron–sulfur clusters) containing sulfide ions, in which the iron ions have variable oxidation states. Pages in category "Iron–sulfur proteins"