The trans-membrane cytochrome b561 Proteins

Structural information and biological function

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Cytochrome b561 (CYB561) proteins are ascorbate reducible, trans-membrane proteins consisting of 200-300 amino acids, about half of which are hydrophobic. The first identified CYB561 protein was discovered more than 40 years ago, and is localized in the chromaffin granule membrane of the mammalian adrenal glands. Proteins with similar structural elements and biophysical and biochemical properties were identified in a wide range of animal and plant phyla in the past 15 years. CYB561 proteins have six trans-membrane helices and two b-type hemes, one on each side of the membrane. The two heme-b centers are coordinated by two pairs of His residues localized in the central four trans-membrane domains, probably very close to the membrane interface. The midpoint redox potentials of the two hemes are above 0 mV and about 100 mV apart from each other. These proteins are different in many respects from the well-known two heme-bcontaining, trans-membrane b-type cytochromes localized in the inner membrane of mitochondria, in the chloroplast thylakoids or in the cell membrane. The atomic-level structure of only one CYB561 protein is available to date. In this paper we discuss in detail the biophysical and biochemical properties of the CYB561 proteins and provide a short overview of their known or putative biological functions and significance.

Original languageEnglish
Pages (from-to)745-760
Number of pages16
JournalCurrent Protein and Peptide Science
Volume15
Issue number8
Publication statusPublished - Dec 1 2014

Fingerprint

Membranes
Heme
Proteins
Cytochrome b Group
Chromaffin Granules
Thylakoids
Mitochondria
Chloroplasts
Cell membranes
Adrenal Glands
cytochrome b561
Oxidation-Reduction
Membrane Proteins
Animals
Cell Membrane
Amino Acids

Keywords

  • Ascorbate
  • Heme-b centers
  • Lipoic acid
  • Point mutants
  • Recombinant proteins
  • Redox potential
  • Spectroscopy

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

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abstract = "Cytochrome b561 (CYB561) proteins are ascorbate reducible, trans-membrane proteins consisting of 200-300 amino acids, about half of which are hydrophobic. The first identified CYB561 protein was discovered more than 40 years ago, and is localized in the chromaffin granule membrane of the mammalian adrenal glands. Proteins with similar structural elements and biophysical and biochemical properties were identified in a wide range of animal and plant phyla in the past 15 years. CYB561 proteins have six trans-membrane helices and two b-type hemes, one on each side of the membrane. The two heme-b centers are coordinated by two pairs of His residues localized in the central four trans-membrane domains, probably very close to the membrane interface. The midpoint redox potentials of the two hemes are above 0 mV and about 100 mV apart from each other. These proteins are different in many respects from the well-known two heme-bcontaining, trans-membrane b-type cytochromes localized in the inner membrane of mitochondria, in the chloroplast thylakoids or in the cell membrane. The atomic-level structure of only one CYB561 protein is available to date. In this paper we discuss in detail the biophysical and biochemical properties of the CYB561 proteins and provide a short overview of their known or putative biological functions and significance.",
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T1 - The trans-membrane cytochrome b561 Proteins

T2 - Structural information and biological function

AU - Bérczi, A.

AU - Zimányi, L.

PY - 2014/12/1

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N2 - Cytochrome b561 (CYB561) proteins are ascorbate reducible, trans-membrane proteins consisting of 200-300 amino acids, about half of which are hydrophobic. The first identified CYB561 protein was discovered more than 40 years ago, and is localized in the chromaffin granule membrane of the mammalian adrenal glands. Proteins with similar structural elements and biophysical and biochemical properties were identified in a wide range of animal and plant phyla in the past 15 years. CYB561 proteins have six trans-membrane helices and two b-type hemes, one on each side of the membrane. The two heme-b centers are coordinated by two pairs of His residues localized in the central four trans-membrane domains, probably very close to the membrane interface. The midpoint redox potentials of the two hemes are above 0 mV and about 100 mV apart from each other. These proteins are different in many respects from the well-known two heme-bcontaining, trans-membrane b-type cytochromes localized in the inner membrane of mitochondria, in the chloroplast thylakoids or in the cell membrane. The atomic-level structure of only one CYB561 protein is available to date. In this paper we discuss in detail the biophysical and biochemical properties of the CYB561 proteins and provide a short overview of their known or putative biological functions and significance.

AB - Cytochrome b561 (CYB561) proteins are ascorbate reducible, trans-membrane proteins consisting of 200-300 amino acids, about half of which are hydrophobic. The first identified CYB561 protein was discovered more than 40 years ago, and is localized in the chromaffin granule membrane of the mammalian adrenal glands. Proteins with similar structural elements and biophysical and biochemical properties were identified in a wide range of animal and plant phyla in the past 15 years. CYB561 proteins have six trans-membrane helices and two b-type hemes, one on each side of the membrane. The two heme-b centers are coordinated by two pairs of His residues localized in the central four trans-membrane domains, probably very close to the membrane interface. The midpoint redox potentials of the two hemes are above 0 mV and about 100 mV apart from each other. These proteins are different in many respects from the well-known two heme-bcontaining, trans-membrane b-type cytochromes localized in the inner membrane of mitochondria, in the chloroplast thylakoids or in the cell membrane. The atomic-level structure of only one CYB561 protein is available to date. In this paper we discuss in detail the biophysical and biochemical properties of the CYB561 proteins and provide a short overview of their known or putative biological functions and significance.

KW - Ascorbate

KW - Heme-b centers

KW - Lipoic acid

KW - Point mutants

KW - Recombinant proteins

KW - Redox potential

KW - Spectroscopy

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