1. Cytochrome c has heme c while other Cytochromes have heme a, b and d

2. Heme is converted by heme oxygenase to Biliverdin, which is then reduced to bilirubin by Biliverdin reductase

3. Biliverdin is a tetrapyrrolic, water-soluble compound formed by the breakdown of heme. Heme is broken down into Biliverdin and carbon monoxide and iron by heme oxidase

4. Biliverdin is a tetrapyrrolic, water-soluble compound formed by the breakdown of heme.[1] Heme is broken down into Biliverdin and carbon monoxide and iron by heme oxidase

5. Heme in TPO (Bassosi et al., 1978)

6. Acetylene alkylates the cytochrome P450 prothestic heme

7. The first step of this process is catalyzed by heme oxygenase, an enzyme that converts heme to iron, carbon monoxide, and Biliverdin.

8. Factors that enhance non-heme iron absorption (22,29):

9. Biliverdin is a linear tetrapyrrole produced in the reticuloendothelial system by the first step of heme degradation, catalysed by heme oxygenase

10. Linear tetrapyrrole compounds (bilins) are derived from the common biosynthetic precursor Biliverdin IXα, which is synthesized from heme by heme oxygenase

11. Biliverdin is a linear tetrapyrrole produced in the reticuloendothelial system by the first step of heme degradation, catalysed by heme oxygenase

12. This causes ineffective heme synthesis and microcytic anemia.

13. Biliverdin is a linear tetrapyrrolic intermediate of heme degradation (heme catabolism) to bilirubin. The bile of amphibia and birds contains only Biliverdine, …

14. The first step of this process is catalyzed by heme oxygenase, an enzyme that converts heme to iron, carbon monoxide, and Biliverdin.

15. Cytochromes are proteins containing one or more heme groups

16. Heme oxygenase or haem oxygenase (HO) is an enzyme that catalyzes the degradation of heme to produce Biliverdin, ferrous iron, and carbon monoxide

17. Studies suggest that Biliverdin hydrochloride can regulate the cellular heme degradation process by inhibiting substrates from binding to the the catalytic site of heme oxygenase.

18. Feosol Complete with Bifera provides both heme and non-heme in a single, small caplet, so you have the flexibility to take it whenever you want

19. Biliverdin is a green pigment that is produced during heme metabolism

20. Heme binding to Albuminoid proteins is the result of recent evolution

21. Biliverdin, a precursor of bilirubin, is one of the three products (the other two are carbon monoxide and free iron) of heme degradation by heme oxygenase‐1 (HO‐1; 10)

22. Cytochrome is an electron-transferring protein with a chemical group called heme

23. But she did find heme, which is the biological foundation of hemoglobin.

24. Heme precursor pattern of human amniotic fluid was analyzed with newer methods.

25. Contrary to early notions, Bilins are not only waste products of heme degradation

26. Meat also contains heme iron, which can facilitate production of Carcinogenic NOCs.

27. Heme group allows the Catalase to react with peroxide in the first place

28. Heme-regulated eukaryotic initiation factor 2 alpha kinase knockout mice and methods for use

29. Bilirubin acts as the pathway that helps to break down the heme present in vertebrates

30. Cytochromes are proteins containing one or more heme groups that are involved in electron transfer

31. Well-known sites of synthesis of chlorophyll for photosynthesis, plant chloroplasts also export heme and heme-derived linear tetrapyrroles (Bilins), two critical metabolites respectively required for essential cellular activities and for light sensing by phytochromes.

32. In Heme, Chlorophyll, and Bilins: Methods and Protocols, an interdisciplinary panel of hands-on investigators describe in detail how to work successfully with chlorophyll, heme, and Bilins in biological, medical, chemical, and biochemical research

33. Cytochromes are enzymes that contain iron in the form of a heme in their active site

34. Catalase is a heme enzyme that is present in the peroxisome of nearly all aerobic cells

35. Catalase is a heme enzyme that is present in the peroxisome of nearly all aerobic cells

36. It arises from enzymatic reduction by Biliverdin reductase of Biliverdin, a product of heme oxygenase activity

37. Bilirubin is an orange-yellow pigment, a waste product primarily produced by the normal breakdown of heme

38. PetJ1 was purified from the cyanobacterium, and both Cytochromes were expressed with heme incorporation in Escherichia coli

39. Significance of heme precursors in human amniotic fluid and its relation to amniotic fluid metabolism is discussed.

40. Approximately 85% of the total Bilirubin produced is derived from the heme moiety of hemoglobin, while the remaining 15% is produced from the red blood cell precursors destroyed in the bone marrow and from the catabolism of other heme-containing proteins

41. Bilirubin is an orange-yellow pigment, a waste product primarily produced by the normal breakdown of heme

42. It contains four iron-containing heme groups that allow the enzyme to react with the hydrogen peroxide.

43. Cytochromes: heme-containing proteins in the electron transport chain that can be alternately in an oxidized or reduced state

44. NOS is the only known enzyme that binds flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), heme, tetrahydrobiopterin (BH4) and calmodulin.

45. Biliverdin is the initial breakdown product of heme, which is further reduced to produce bilirubin. Using surface plasmon resonance, they …

46. In science, Artemisinin has an endoperoxide capacity, that interacts with heme, especially in situations that increase iron in cancer cells

47. Azide is a potent inhibitor of mitochondrial respiration that blocks cytochrome c oxidase by binding between the heme a 3 iron and Cu B in the oxygen reduction site (2, 3).Many other heme proteins and other metalloenzymes are inhibited by Azide binding to their metal centers.

48. Cytochromes can be distinguished by: Spectroscopy, exact structure of the heme group, inhibitor sensitivity, reduction potential Prosthetic group for Cytochrome a:

49. Specifically, Cyanide binds to the heme a3-CuB binuclear center of COX (and thus is a non-competitive inhibitor of it).

50. Cytochromes are electron-transporting protein pigments concerned with cell respiration that contain an iron-containing molecule called heme, allied to that of hemoglobin

51. The function of Cytochromes as electron carriers involves the alternate oxidation and reduction of the iron ion present in the heme group, one

52. Cytochromes are hemeproteins containing heme groups and are primarily responsible for the generation of ATP via electron transport.They are found either as m

53. What does Cytochrome mean? Any of a class of usually colored proteins that contain a heme group, are electron carriers, and catalyze oxidation-redu

54. Carbon monoxide is a gas produced by the combustion of hydrocarbon products that binds to heme molecules, 240 times more than oxygen, producing Carboxyhemoglobin (COHb)

55. And they indicated that the sulphur atom of these drugs may coordinate to the metal center of active site heme in TPO (Bassosi et al., 1978)

56. In the Electron Transport Chain, Cytochrome c transfers one electron at a time via its heme group from the third complex of the electron transport chain,

57. However, in the case of monosubstituted Acetylenes, inactivation can also occur by addition of the oxidized acetylenic function to a nitrogen of the heme prosthetic group

58. Biliverdin heme iron cahmx1 disease Prior art date 2004-03-19 Legal status (The legal status is an assumption and is not a legal conclusion

59. The basic structure of Chlorophyll is a porphyrin ring similar to that of heme in hemoglobin, although the central atom in Chlorophyll is magnesium instead of iron

60. The Cytochrome oxidase of eukaryotes is a very complex protein assembly containing from 8 to 13 polypeptide subunits, two hemes, a and a 3, and two atoms of copper.The two hemes are chemically identical but are placed in different protein environments, so that heme a can accept an electron from Cytochrome c and heme a 3 can react with oxygen.

61. Cytochromes are identified by the type of heme moiety present (a, b, c, or d), and the wavelength of maximal absorbance of the Soret band (e.g., cytochrome b 559)

62. When countering malaria, Artemisinin exploits the parasite’s taste for hemoglobin in its host’s blood. As the parasite digests hemoglobin, it frees the iron-porphyrin heme complex from the protein

63. A-type Cytochromes • Heme a, found in a- type Cytochromes, has a long isoprenoid tail substituted on one of the vinyl groups and a formyl group replacing a methyl

64. The activity enhancement upon heme binding is therefore an Allosteric effect likely linked to dynamics, as it is the case with other Allosteric effects reported in the literature 53

65. Cofactors are divided into two broad groups: Organic Cofactors, such as flavin or heme, Inorganic Cofactors, such as metal ions (Mg 2+, Cu 2+, Mn 2+), or iron-sulfur clusters

66. The elucidation of enigmatic enzymatic chlorination timing in Ambiguine indole alkaloid biogenesis led to the discovery and characterization of AmbO5 protein as a promiscuous non‐heme iron aliphatic halogenase

67. Cytochrome c is a highly conserved ~12 kDa protein consisting of a single 104 amino acid peptide with a single heme group, which is covalently attached to Cys and Cys

68. Sodium Bisulfide treatment raised the activity of superoxide dismutase (SOD) and heme oxygenase-1 (HO-1) protein expression, and decreased tumor necrosis factor α (TNF-α) protein expression in diabetic rats

69. Bination subsumes b oth the non-resonan recom Bination (\radiativ e Bination"), and the resonan t Bination (\di-electronic re-com Bination") pro cesses in a uni ed sc heme

70. We have found that although both HbA and HbE Autoxidize at initially comparable rates, HbE loses heme at a rate almost 2 fold higher than HbA due to unfolding of the protein

71. Cytochromes are a class of electron-transferring metalloproteins containing a heme as prosthetic group, and that participate in many different respiratory and photosynthetic electron transport chains, usually as membrane-bound electron carriers

72. Their Biosyntheses involve an unprecedented trans-sulfur strategy, a combination of a mononuclear non-heme iron enzyme-catalyzed oxidative C–S bond formation reaction and a PLP enzyme-mediated C–S lyase reaction

73. When the iron of heme accepts an electron, it changes from the oxidized ferric (Fe III) state to the reduced ferrous (Fe II) state.The oxidation of Cytochromes to molecular oxygen and their subsequent reduction by oxidizable

74. Hb Bibba alpha136(H19)Leu->Pro ; CONTACT: Heme contact: HEMATOLOGY: Hemolytic anemia in the heterozygote: ELECTROPHORESIS: Hb X moves like Hb S in IEF and electrophoresis at alkaline pH; freshly collected blood is required: CHROMATOGRAPHY: Hb X was …

75. Catalase is a tetrameric heme protein and detoxifies H2 O 2 into oxygen and water. It is a metalloprotein oxidoreductase enzyme and efficiently scavenges H 2 O 2 when it is present in high concentrations (Day 2009, Cao et al., 2003)

76. Definition of Biliverdin : a green pigment that occurs in bile and is an intermediate in the degradation of hemoglobin heme groups to bilirubin Examples of Biliverdin in a Sentence Recent Examples on the Web The substance making these little reptiles viridescent is Biliverdin, …

77. Catalase (EC 1.11.1.6) is an enzyme which is present mainly in the peroxisomes of mammalian cells. It is a tetrameric enzyme consisting of four identical, tetrahedrally arranged subunits of 60 kDa, each containing in its active center a heme group and NADPH

78. Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric Cytochrome c peroxidase from yeast: effects of sample history and pH1The reviewing and handling of this manuscript was overseen by a member of the editorial board.1.

79. Timely and highly practical, Heme, Chlorophyll, and Bilins: Methods and Protocols is a gold-standard collection of readily reproducible techniques suitable for a wide range of researchers, whether it be a clinician studying photodynamic therapy, an ecologist studying the chlorophyll composition of leaves in a tropical forest, or a cell

80. Bilirubin [bil″ĭ-roo´bin] a yellow to orange bile pigment produced by the breakdown of heme and reduction of biliverdin; it normally circulates in plasma and is taken up by liver cells and conjugated to form Bilirubin diglucuronide, the water-soluble pigment excreted in the bile