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  2. Hemoprotein - Wikipedia

    en.wikipedia.org/wiki/Hemoprotein

    Electron transport proteins [29] Oxygen transport proteins [30] Photosensitive proteins [25] Design techniques have matured to such an extent that it is now possible to generate entire libraries of heme binding helical proteins. [31] Recent design attempts have focused on creating all-beta heme binding proteins, whose novel topology is very ...

  3. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ HEEM), is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. [1] Heme is biosynthesized in both the bone marrow and ...

  4. Heme C - Wikipedia

    en.wikipedia.org/wiki/Heme_C

    The number of heme C units bound to a holoprotein is highly variable. For vertebrate cells one heme C per protein is the rule but for bacteria this number is often 2, 4, 5, 6 or even 16 heme C groups per holoprotein. It is generally agreed the number and arrangement of heme C groups are related and even required for proper holoprotein function.

  5. Cytochrome - Wikipedia

    en.wikipedia.org/wiki/Cytochrome

    He classified these heme proteins on the basis of the position of their lowest energy absorption band in their reduced state, as cytochromes a (605 nm), b (≈565 nm), and c (550 nm). The ultra-violet (UV) to visible spectroscopic signatures of hemes are still used to identify heme type from the reduced bis-pyridine-ligated state, i.e., the ...

  6. Cytochrome P450 - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_P450

    Molecular oxygen binds to the resulting ferrous heme center at the distal axial coordination position, initially giving a dioxygen adduct similar to oxy-myoglobin. A second electron is transferred, from either cytochrome P450 reductase, ferredoxins, or cytochrome b 5, reducing the Fe-O 2 adduct to give a short-lived peroxo state.

  7. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    Such a name is given because this arrangement is the same folding motif used in other heme/globin proteins such as myoglobin. [45] [46] This folding pattern contains a pocket that strongly binds the heme group. [citation needed] A heme group consists of an iron (Fe) ion held in a heterocyclic ring, known as a porphyrin.

  8. Category:Hemoproteins - Wikipedia

    en.wikipedia.org/wiki/Category:Hemoproteins

    Heme-thiolate proteins (1 C, 1 P) Hemoglobins (38 P) Pages in category "Hemoproteins" The following 22 pages are in this category, out of 22 total.

  9. Heme B - Wikipedia

    en.wikipedia.org/wiki/Heme_B

    Heme B or haem B (also known as protoheme IX) is the most abundant heme. [1] Hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. The COX-1 and COX-2 enzymes (cyclooxygenase) of recent fame, also contain heme B at one of two active sites.