NDLI: Significantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobin.

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Significantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Uppal, Sheetal Mukhi, Nitika Kundu, Suman Dey, Somdatta Ghosh Zaidi, Fatima Kamal Bhat, Rajiv Salhotra, Shikha Seal, Manas
Description	Author Affiliation: Uppal S ( From the Department of Biochemistry, University of Delhi South Campus, New Delhi 110021, India.); Salhotra S ( From the Department of Biochemistry, University of Delhi South Campus, New Delhi 110021, India.); Mukhi N ( From the Department of Biochemistry, University of Delhi South Campus, New Delhi 110021, India.); Zaidi FK ( the School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India, and.); Seal M ( the Department of Inorganic Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata 700032, India.); Dey SG ( the Department of Inorganic Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata 700032, India.); Bhat R ( the School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India, and.); Kundu S ( From the Department of Biochemistry, University of Delhi South Campus, New Delhi 110021, India, suman.kundu@south.du.ac.in.)
Abstract	Heme proteins, which reversibly bind oxygen and display a particular fold originally identified in myoglobin (Mb), characterize the 'hemoglobin (Hb) superfamily.' The long known and widely investigated Hb superfamily, however, has been enriched by the discovery and investigation of new classes and members. Truncated Hbs typify such novel classes and exhibit a distinct two-on-two -helical fold. The truncated Hb from the freshwater cyanobacterium Synechocystis exhibits hexacoordinate heme chemistry and bears an unusual covalent bond between the nonaxial His(117) and a heme porphyrin 2-vinyl atom, which remains tightly associated with the globin unlike any other. It seems to be the most stable Hb known to date, and His(117) is the dominant force holding the heme. Mutations of amino acid residues in the vicinity did not influence this covalent linkage. Introduction of a nonaxial His into sperm whale Mb at the topologically equivalent position and in close proximity to vinyl group significantly increased the heme stability of this prototype globin. Reversed phase chromatography, electrospray ionization-MS, and MALDI-TOF analyses confirmed the presence of covalent linkage in Mb I107H. The Mb mutant with the engineered covalent linkage was stable to denaturants and exhibited ligand binding and auto-oxidation rates similar to the wild type protein. This indeed is a novel finding and provides a new perspective to the evolution of Hbs. The successful attempt at engineering heme stability holds promise for the production of stable Hb-based blood substitute.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	4
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-01-23
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Histidine Chemistry Myoglobin Protein Engineering Synechocystis Amino Acid Sequence Calorimetry, Differential Scanning Circular Dichroism Electron Spin Resonance Spectroscopy Escherichia Coli Metabolism Heme Hemoglobins Hydrogen-Ion Concentration Molecular Sequence Data Mutagenesis, Site-Directed Mutation Recombinant Proteins Sequence Homology, Amino Acid Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Truncated Hemoglobins Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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