A mechanistic and electrochemical study of the interaction between dimethyl sulfide dehydrogenase and its electron transfer partner cytochrome c2

Creevey, N.; McEwan, A.; Bernhardt, P.; J. Biol. Inorg. Chem. 13, 1231-1238 (2008)

Data extracted from this reference:

KM Value [mM]

KM Value Maximum [mM]

Substrate

Commentary

Organism

Structure

0.021

-

ferricytochrome c2

in 220 mM Tris-HCl pH 8.0, 22°C

Rhodovulum sulfidophilum

0.053

-

Dimethyl sulfide

in 220 mM Tris-HCl pH 8.0, 22°C

Rhodovulum sulfidophilum

Natural Substrates

Organism

Commentary (Nat. Sub.)

Natural Products

Commentary (Nat. Pro.)

Organism (Nat. Pro.)

Reversibility

ID

dimethyl sulfide + ferricytochrome c2 + H2O

Rhodovulum sulfidophilum

-

dimethyl sulfoxide + ferrocytochrome c2

-

-

?

dimethyl sulfide + ferricytochrome c2 + H2O

Rhodovulum sulfidophilum SH1

-

dimethyl sulfoxide + ferrocytochrome c2

-

-

?

Substrates

Commentary Substrates

Literature (Substrates)

Organism

Products

Commentary (Products)

Literature (Products)

Organism (Products)

Reversibility

Substrate Product ID

dimethyl sulfide + ferricytochrome c2 + H2O

-

715664

Rhodovulum sulfidophilum

dimethyl sulfoxide + ferrocytochrome c2

-

-

-

?

dimethyl sulfide + ferricytochrome c2 + H2O

DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism

715664

Rhodovulum sulfidophilum

dimethyl sulfoxide + ferrocytochrome c2

-

-

-

?

dimethyl sulfide + ferricytochrome c2 + H2O

-

715664

Rhodovulum sulfidophilum SH1

dimethyl sulfoxide + ferrocytochrome c2

-

-

-

?

dimethyl sulfide + ferricytochrome c2 + H2O

DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism

715664

Rhodovulum sulfidophilum SH1

dimethyl sulfoxide + ferrocytochrome c2

-

-

-

?

Cofactor

Commentary

Organism

Structure

heme

the enzyme contains a heme b cofactor

Rhodovulum sulfidophilum

iron-sulfur centre

the enzyme contains five iron-sulfur clusters

Rhodovulum sulfidophilum

molybdopterin

-

Rhodovulum sulfidophilum

Cofactor

Commentary

Organism

Structure

heme

the enzyme contains a heme b cofactor

Rhodovulum sulfidophilum

iron-sulfur centre

the enzyme contains five iron-sulfur clusters

Rhodovulum sulfidophilum

molybdopterin

-

Rhodovulum sulfidophilum

KM Value [mM]

KM Value Maximum [mM]

Substrate

Commentary

Organism

Structure

0.021

-

ferricytochrome c2

in 220 mM Tris-HCl pH 8.0, 22°C

Rhodovulum sulfidophilum

0.053

-

Dimethyl sulfide

in 220 mM Tris-HCl pH 8.0, 22°C

Rhodovulum sulfidophilum

Natural Substrates

Organism

Commentary (Nat. Sub.)

Natural Products

Commentary (Nat. Pro.)

Organism (Nat. Pro.)

Reversibility

ID

dimethyl sulfide + ferricytochrome c2 + H2O

Rhodovulum sulfidophilum

-

dimethyl sulfoxide + ferrocytochrome c2

-

-

?

dimethyl sulfide + ferricytochrome c2 + H2O

Rhodovulum sulfidophilum SH1

-

dimethyl sulfoxide + ferrocytochrome c2

-

-

?

Substrates

Commentary Substrates

Literature (Substrates)

Organism

Products

Commentary (Products)

Literature (Products)

Organism (Products)

Reversibility

ID

dimethyl sulfide + ferricytochrome c2 + H2O

-

715664

Rhodovulum sulfidophilum

dimethyl sulfoxide + ferrocytochrome c2

-

-

-

?

dimethyl sulfide + ferricytochrome c2 + H2O

DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism

715664

Rhodovulum sulfidophilum

dimethyl sulfoxide + ferrocytochrome c2

-

-

-

?

dimethyl sulfide + ferricytochrome c2 + H2O

-

715664

Rhodovulum sulfidophilum SH1

dimethyl sulfoxide + ferrocytochrome c2

-

-

-

?

dimethyl sulfide + ferricytochrome c2 + H2O

DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism

715664

Rhodovulum sulfidophilum SH1

dimethyl sulfoxide + ferrocytochrome c2

-

-

-

?

No.

1st author

Pub Med

title

organims

journal

volume

pages

year

Activating Compound

Application

Cloned(Commentary)

Crystallization (Commentary)

Engineering

General Stability

Inhibitors

KM Value [mM]

Localization

Metals/Ions

Molecular Weight [Da]

Natural Substrates/ Products (Substrates)

Organic Solvent Stability

Organism

Oxidation Stability

Posttranslational Modification

Purification (Commentary)

Reaction

Renatured (Commentary)

Source Tissue

Specific Activity [micromol/min/mg]

Storage Stability

Substrates and Products (Substrate)

Subunits

Synonyms

Temperature Optimum [°C]

Temperature Range [°C]

Temperature Stability [°C]

Turnover Number [1/s]

pH Optimum

pH Range

pH Stability

Cofactor

Ki Value [mM]

pI Value

IC50 Value

Activating Compound (protein specific)

Application (protein specific)

Cloned(Commentary) (protein specific)

Cofactor (protein specific)

Crystallization (Commentary) (protein specific)

Engineering (protein specific)

General Stability (protein specific)

IC50 Value (protein specific)

Inhibitors (protein specific)

Ki Value [mM] (protein specific)

KM Value [mM] (protein specific)

Localization (protein specific)

Metals/Ions (protein specific)

Molecular Weight [Da] (protein specific)

Natural Substrates/ Products (Substrates) (protein specific)

Organic Solvent Stability (protein specific)

Oxidation Stability (protein specific)

Posttranslational Modification (protein specific)

Purification (Commentary) (protein specific)

Renatured (Commentary) (protein specific)

Source Tissue (protein specific)

Specific Activity [micromol/min/mg] (protein specific)

Storage Stability (protein specific)

Substrates and Products (Substrate) (protein specific)

Subunits (protein specific)

Temperature Optimum [°C] (protein specific)

Temperature Range [°C] (protein specific)

Temperature Stability [°C] (protein specific)

Turnover Number [1/s] (protein specific)

pH Optimum (protein specific)

pH Range (protein specific)

pH Stability (protein specific)

pI Value (protein specific)

Expression

General Information

General Information (protein specific)

Expression (protein specific)

KCat/KM [mM/s]

KCat/KM [mM/s] (protein specific)

715664

Creevey

A mechanistic and electrochemi ...

Rhodovulum sulfidophilum, Rhodovulum sulfidophilum SH1

J. Biol. Inorg. Chem.

13

1231-1238

2008

-

-

-

-

-

-

-

2

-

-

-

2

-

9

-

-

1

-

-

-

-

-

4

1

3

-

-

-

-

1

-

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3

-

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-

-

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3

-

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2

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-

2

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1

-

-

-

-

4

1

-

-

-

-

1

-

-

-

-

-

-

-

-

-

716248

McDevitt

Molecular analysis of dimethyl ...

Rhodovulum sulfidophilum, Rhodovulum sulfidophilum SH1

Mol. Microbiol.

44

1575-1587

2002

-

-

-

-

-

-

-

-

3

6

9

6

-

13

-

-

3

-

-

-

-

-

12

3

12

-

-

-

-

-

-

-

4

-

-

-

-

-

-

4

-

-

-

-

-

-

-

3

6

9

6

-

-

-

3

-

-

-

-

12

3

-

-

-

-

-

-

-

-

-

4

4

-

-

-

714886

Hanlon

Dimethylsulfide: acceptor oxid ...

Rhodovulum sulfidophilum

Eur. J. Biochem.

239

391-396

1996

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1

2

4

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1

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1

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5

1

2

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3

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3

-

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-

1

2

4

-

-

-

-

1

-

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2

-

5

1

-

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-

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