1UFP

Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-wild type Myoglobin

Summary for 1UFP

• Entry DOI: 10.2210/pdb1ufp/pdb
• Related: 1UFJ
• Descriptor: Myoglobin, PHOSPHATE ION (3 entities in total)
• Functional Keywords: myoglobin, schiff base, iron, salophen, metalloprotein, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Physeter catodon (sperm whale)
• Total number of polymer chains: 1
• Total formula weight: 17935.97

Authors

Ueno, T.,Ohashi, M.,Kono, M.,Kondo, K.,Suzuki, A.,Yamane, T.,Watanabe, Y. (deposition date: 2003-06-04, release date: 2004-05-18, Last modification date: 2023-11-08)

Primary citation

Ueno, T.,Ohashi, M.,Kono, M.,Kondo, K.,Suzuki, A.,Yamane, T.,Watanabe, Y.
Crystal Structures of Artificial Metalloproteins: Tight Binding of Fe(III)(Schiff-Base) by Mutation of Ala71 to Gly in Apo-Myoglobin
Inorg.Chem., 43:2852-2858, 2004

PubMed Abstract: Apo-myoglobin (apo-Mb) and apo-A71GMb were successfully reconstituted with FeIII(salophen) (1) (salophen = N,N'-bis(salicylidene)-1,2-phenilenediamine), Fe(III)(3,3'-Me2-salophen) (2), and FeIII(5,5'-t-Bu2-salophen) (3). The crystal structure of 2.apo-A71GMb shows the tight binding of the complex in the Mb cavity, while in wild-type apo-Mb it is highly disordered due to the steric repulsion with Ala71. Furthermore, the structure of 2.apo-A71GMb suggests a possible accommodation of a small substrate in the cavity. In fact, the cyanide association rate constant of 2.apo-A71GMb is 216-fold larger compared to that of 2.apo-Mb. These results provide us principles for the noncovalent fixation of synthetic metal cofactors at the desired positions in protein matrixes.

PubMed: 15106972
DOI: 10.1021/ic0498539

Experimental method

X-RAY DIFFRACTION (2.1 Å)