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for advanced users..:P Did anyone know what happens if we substitute one of the cysteines of ribonucleotide reductase's with a methionine??

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Those things are quite hard to predict. It depends a lot on the precise structure of the given reductase, where the location of the cysteine is in question etc.

The main point is that methionine does not form disulfide bonds, so that is likely to change the structure, but it depends which of the S-S bonds being disrupted, of course.

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it says in the question that is one of the two cysteines of the active center of the enzyme..so you say that its basic function (which is to tranform ribonucleotides to deoxyribonucleotides)will be canceled?

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