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The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_70642026

The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

About this item

Full title

The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

Publisher

New York: Nature Publishing Group US

Journal title

Nature Structural Biology, 2001-02, Vol.8 (2), p.156-160

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Human ferrochelatase (E.C. 4.99.1.1) is a homodimeric (86 kDa) mitochondrial membrane-associated enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme. We have determined the 2.0 Å structure from the single wavelength iron anomalous scattering signal. The enzyme contains two NO-sensitive and uniquely coordinated [2Fe-...

Alternative Titles

Full title

The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_70642026

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_70642026

Other Identifiers

ISSN

1072-8368,1545-9993

E-ISSN

1545-9985

DOI

10.1038/84152

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