4 Citations (Scopus)

Abstract

The ancient metabolism of photoferrotrophy is likely to have played a key role in the biogeochemical cycle of iron on Early Earth leading to the deposition of Banded Iron Formations prior to the emergence of oxygenic photosynthesis. Extant organisms still performing this metabolism provide a convenient window to peer into its molecular mechanisms. Here we report the molecular structure of FoxE, the putative terminal iron oxidase of Rhodobacter ferrooxidans SW2. This protein is organized as a trimer with two hemes and a disulfide bridge per monomer. The distance between hemes, their solvent exposure and the surface electrostatics ensure a controlled electron transfer rate. They also guarantee segregation between electron capture from ferrous iron and electron release to downstream acceptors, which do not favor the precipitation of ferric iron. Combined with the functional characterization of this protein, the structure reveals how iron oxidation can be performed in the periplasmic space of this Gram-negative bacterium at circumneutral pH, while minimizing the risk of mineral precipitation and cell encrustation.

Original languageEnglish
Pages (from-to)847-853
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1858
Issue number10
DOIs
Publication statusPublished - 1 Oct 2017

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Rhodobacter
Molecular Structure
Molecular structure
Oxidoreductases
Iron
Electrons
Metabolism
Periplasm
Photosynthesis
Gram-Negative Bacteria
Static Electricity
Heme
Disulfides
Minerals
Electrostatics
Bacteria
Proteins
Monomers
Earth (planet)
Oxidation

Keywords

  • Crystallography
  • Cytochrome
  • Electron transfer
  • Photoferrotrophy
  • Surface electrostatics

Cite this

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title = "Molecular structure of FoxE, the putative iron oxidase of Rhodobacter ferrooxidans SW2",
abstract = "The ancient metabolism of photoferrotrophy is likely to have played a key role in the biogeochemical cycle of iron on Early Earth leading to the deposition of Banded Iron Formations prior to the emergence of oxygenic photosynthesis. Extant organisms still performing this metabolism provide a convenient window to peer into its molecular mechanisms. Here we report the molecular structure of FoxE, the putative terminal iron oxidase of Rhodobacter ferrooxidans SW2. This protein is organized as a trimer with two hemes and a disulfide bridge per monomer. The distance between hemes, their solvent exposure and the surface electrostatics ensure a controlled electron transfer rate. They also guarantee segregation between electron capture from ferrous iron and electron release to downstream acceptors, which do not favor the precipitation of ferric iron. Combined with the functional characterization of this protein, the structure reveals how iron oxidation can be performed in the periplasmic space of this Gram-negative bacterium at circumneutral pH, while minimizing the risk of mineral precipitation and cell encrustation.",
keywords = "Crystallography, Cytochrome, Electron transfer, Photoferrotrophy, Surface electrostatics",
author = "Luis Pereira and Saraiva, {Ivo H.} and Oliveira, {A. Sofia F.} and Soares, {Cl{\'a}udio M.} and Louro, {Ricardo O.} and Carlos Fraz{\~a}o",
year = "2017",
month = "10",
day = "1",
doi = "10.1016/j.bbabio.2017.07.002",
language = "English",
volume = "1858",
pages = "847--853",
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TY - JOUR

T1 - Molecular structure of FoxE, the putative iron oxidase of Rhodobacter ferrooxidans SW2

AU - Pereira, Luis

AU - Saraiva, Ivo H.

AU - Oliveira, A. Sofia F.

AU - Soares, Cláudio M.

AU - Louro, Ricardo O.

AU - Frazão, Carlos

PY - 2017/10/1

Y1 - 2017/10/1

N2 - The ancient metabolism of photoferrotrophy is likely to have played a key role in the biogeochemical cycle of iron on Early Earth leading to the deposition of Banded Iron Formations prior to the emergence of oxygenic photosynthesis. Extant organisms still performing this metabolism provide a convenient window to peer into its molecular mechanisms. Here we report the molecular structure of FoxE, the putative terminal iron oxidase of Rhodobacter ferrooxidans SW2. This protein is organized as a trimer with two hemes and a disulfide bridge per monomer. The distance between hemes, their solvent exposure and the surface electrostatics ensure a controlled electron transfer rate. They also guarantee segregation between electron capture from ferrous iron and electron release to downstream acceptors, which do not favor the precipitation of ferric iron. Combined with the functional characterization of this protein, the structure reveals how iron oxidation can be performed in the periplasmic space of this Gram-negative bacterium at circumneutral pH, while minimizing the risk of mineral precipitation and cell encrustation.

AB - The ancient metabolism of photoferrotrophy is likely to have played a key role in the biogeochemical cycle of iron on Early Earth leading to the deposition of Banded Iron Formations prior to the emergence of oxygenic photosynthesis. Extant organisms still performing this metabolism provide a convenient window to peer into its molecular mechanisms. Here we report the molecular structure of FoxE, the putative terminal iron oxidase of Rhodobacter ferrooxidans SW2. This protein is organized as a trimer with two hemes and a disulfide bridge per monomer. The distance between hemes, their solvent exposure and the surface electrostatics ensure a controlled electron transfer rate. They also guarantee segregation between electron capture from ferrous iron and electron release to downstream acceptors, which do not favor the precipitation of ferric iron. Combined with the functional characterization of this protein, the structure reveals how iron oxidation can be performed in the periplasmic space of this Gram-negative bacterium at circumneutral pH, while minimizing the risk of mineral precipitation and cell encrustation.

KW - Crystallography

KW - Cytochrome

KW - Electron transfer

KW - Photoferrotrophy

KW - Surface electrostatics

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U2 - 10.1016/j.bbabio.2017.07.002

DO - 10.1016/j.bbabio.2017.07.002

M3 - Article

VL - 1858

SP - 847

EP - 853

JO - Biochimica Et Biophysica Acta-Bioenergetics

JF - Biochimica Et Biophysica Acta-Bioenergetics

SN - 0005-2728

IS - 10

ER -