I know that metal ions are present in enzymes, and that this affects their stability and function.
However, when producing or engineering enzymes, I wonder if metal ions have a negative effect.
Metal ions are interacting with cysteine and histidine in proteins such as zinc finger and ring domain.
Are there cases where cysteine and histidine are replaced with other amino acids to remove metal ions and maintain the structure?
Metals when present in proteins are there for an evolved reason; usually structural and/or catalytic function. Both HEW and T4 lysozyme have an extensive history of the impact of various metals in their structure and function, so maybe review that literature. The only "problem" I could see from metals might be partial or mixed residency and this giving a mixed population of enzymatic activities, complicating analyses. Many enzymes have been studied by chelating out one metal and then adding back another, see this paper and refs therin. Article The Case for Enzymatic Competitive Metal Affinity Methods
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